|
Name |
Accession |
Description |
Interval |
E-value |
| PH_ROCK |
cd01242 |
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ... |
466-572 |
6.08e-58 |
|
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269948 Cd Length: 110 Bit Score: 191.41 E-value: 6.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 466 SRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQI 545
Cdd:cd01242 1 SRLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQI 80
|
90 100 110
....*....|....*....|....*....|
gi 109730369 546 LYANEGESKKEQEFPVE---PVGEKSNYIC 572
Cdd:cd01242 81 LYANEGESSRPAEVTDTlsvSREEKPNTIL 110
|
|
| C1_ROCK2 |
cd20875 |
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ... |
565-635 |
3.72e-55 |
|
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410425 Cd Length: 71 Bit Score: 182.54 E-value: 3.72e-55
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109730369 565 GEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYD 635
Cdd:cd20875 1 GEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVNYD 71
|
|
| C1_ROCK1 |
cd20874 |
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ... |
569-637 |
2.82e-47 |
|
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410424 Cd Length: 69 Bit Score: 160.95 E-value: 2.82e-47
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109730369 569 NYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDIS 637
Cdd:cd20874 1 NFLPHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDMITPCKVNYDVT 69
|
|
| C1_ROCK |
cd20813 |
protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil ... |
569-633 |
9.12e-40 |
|
protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil containing protein kinase (ROCK) family; ROCK is a serine/threonine protein kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410363 Cd Length: 65 Bit Score: 140.10 E-value: 9.12e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109730369 569 NYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVY 633
Cdd:cd20813 1 GTISHKGHEFVEITFHMPTTCDVCHKPLWHLFKPPPALECKRCRMKIHKDHVDKEEYFIPPCKVN 65
|
|
| ROCK_SBD |
cd22250 |
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ... |
171-251 |
3.08e-28 |
|
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) region encompassing a Rho-binding domain (RBD), and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.
Pssm-ID: 409019 [Multi-domain] Cd Length: 75 Bit Score: 107.73 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 171 DGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKlgkelqQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQ 250
Cdd:cd22250 1 DLQMKELQDQLEAEQYFSTLYKTQVKELKEELEEKTR------QIKQELEDERESLSAQLELALAKADSEQLARSIAEEQ 74
|
.
gi 109730369 251 Y 251
Cdd:cd22250 75 I 75
|
|
| Rho_Binding |
pfam08912 |
Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding ... |
294-361 |
1.23e-20 |
|
Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding domain-containing proteins (such as ROCK) to Rho, resulting in activation of the GTPase which in turn modulates the phosphorylation of various signalling proteins. This domain is within an amphipathic alpha-helical coiled-coil and interacts with Rho through predominantly hydrophobic interactions.
Pssm-ID: 462630 [Multi-domain] Cd Length: 68 Bit Score: 86.17 E-value: 1.23e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109730369 294 TSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKE 361
Cdd:pfam08912 1 TKDVENLAKEKEELNNKLKEQQEELEKAKEEEEEIEKLKASYEKQLNTERTLKTQAVNKLAEIMNRKD 68
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-479 |
1.45e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 90 INELLKQKDVLNEDVRN----LTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRK 165
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 166 ERQDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEitltkADSEQLARs 245
Cdd:COG1196 275 ELEELELELEEAQAEEYELL-------AELARLEQDIARLEERRRELEERLEELEEELAELEEELE-----ELEEELEE- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 246 iAEEQYSDLEKEKIMKELEIKEmmarHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEE 325
Cdd:COG1196 342 -LEEELEEAEEELEEAEAELAE----AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 326 ISAAAIKAQFEKQLLTERTLKTQAVNKLAEImnrkepvkrgndtdvRRKEKENRKLHMELKSEREKLTQQMIKYQKELNE 405
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEA---------------AEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109730369 406 MQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNN 479
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| C1 |
smart00109 |
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
576-622 |
6.81e-14 |
|
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.
Pssm-ID: 197519 Cd Length: 50 Bit Score: 66.34 E-value: 6.81e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMDK 622
Cdd:smart00109 1 HKHVFRTFTKPTFCCVCRKSIWGSFK--QGLRCSECKVKCHKKCADK 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
89-361 |
2.16e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 89 KINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQ 168
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 169 DADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAE 248
Cdd:COG1196 313 ELEERLEELEEELAELE-------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 249 EQYSDLEKEKIMKELEIKEMMARHKQELTEkdatIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISA 328
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270
....*....|....*....|....*....|...
gi 109730369 329 AAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKE 361
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-441 |
2.71e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 156 LEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLT 235
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 236 KADSEQLARSIAEEQYSDLEK--EKIMKELE-IKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLK 312
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAqiEQLKEELKaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 313 DVQEQLSRLKDEEISAAAIKAQFEKQLlterTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKL 392
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 109730369 393 TQ---QMIKYQKELNEMQAQIAEESQIRIELQMTLDSK-DSDIEQLRSQLQAL 441
Cdd:TIGR02168 925 AQlelRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRL 977
|
|
| C1 |
cd00029 |
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
576-630 |
5.16e-13 |
|
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.
Pssm-ID: 410341 Cd Length: 50 Bit Score: 63.69 E-value: 5.16e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMDKkeeIIAPC 630
Cdd:cd00029 1 HRFVPTTFSSPTFCDVCGKLIWGLFK--QGLKCSDCGLVCHKKCLDK---APSPC 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-329 |
4.34e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVEnllleaekrcslldcdlkqsq 87
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA--------------------- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 qkinELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKER 167
Cdd:COG1196 299 ----RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 168 QDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIA 247
Cdd:COG1196 375 AEAEEELEELAEELLEAL-------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 248 EEQYSDLEKEkimkELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEIS 327
Cdd:COG1196 448 AEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
..
gi 109730369 328 AA 329
Cdd:COG1196 524 GA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-358 |
1.58e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 22 EHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRcslldcdLKQSQQKINELLKQKDVLN 101
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 102 EDVRNLTLKIEQetqkrclTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQL 181
Cdd:TIGR02168 309 ERLANLERQLEE-------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 182 EaeqyfstlykTQVRELKEECEEKTKLGKELQQKKQELqderdslaaqleitltkadsEQLARSIAEEQYSDLEKEKIMK 261
Cdd:TIGR02168 382 E----------TLRSKVAQLELQIASLNNEIERLEARL--------------------ERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 262 ELEIKEmmarHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFE----- 336
Cdd:TIGR02168 432 EAELKE----LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfseg 507
|
330 340
....*....|....*....|...
gi 109730369 337 -KQLLTERTLKTQAVNKLAEIMN 358
Cdd:TIGR02168 508 vKALLKNQSGLSGILGVLSELIS 530
|
|
| PH_MRCK |
cd01243 |
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ... |
469-545 |
1.80e-11 |
|
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269949 Cd Length: 135 Bit Score: 62.31 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 469 EGWLSLPVRNNTKKfGWVKKYVIVSSKKILFYDSEQDKEQS---NPYMVLDI-DKLFHVRPVTQTDVYRADAKEIPRIFQ 544
Cdd:cd01243 15 EGYVRVPKPGGVKK-GWQRQFAVVCDFKLFLFDISEDKASQpsqVASQVLDMrDEEFSVSSVLASDVIHANKKDIPCIFR 93
|
.
gi 109730369 545 I 545
Cdd:cd01243 94 V 94
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-359 |
3.64e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 14 QSLEQEEAEHKATKARLADKnkiyesiEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINEL 93
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEK-------IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 94 LKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQ 173
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 174 MKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSD 253
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 254 LEKEKIMKE---LEIKEMMARHKQELTEKDATIASLEETNRTLTSDVA-NLANEKEELNNKLKDVQEQLSRLKDE----- 324
Cdd:TIGR02168 906 LESKRSELRrelEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeEAEALENKIEDDEEEARRRLKRLENKikelg 985
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 109730369 325 EISAAAIkAQFEKQ------LLTERTLKTQAVNKLAEIMNR 359
Cdd:TIGR02168 986 PVNLAAI-EEYEELkerydfLTAQKEDLTEAKETLEEAIEE 1025
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-441 |
4.32e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 84 KQSQQKINE----LLKQKDVLNEDVRNLtlkieqetqkrcltqNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMN-LEK 158
Cdd:TIGR02168 175 KETERKLERtrenLDRLEDILNELERQL---------------KSLERQAEKAERYKELKAELRELELALLVLRLEeLRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 159 QNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQderdslaaqLEITLTKAD 238
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---------QQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 239 SEQLARSIAEEQYSDLEKEKimKELEIKEMMARHKQELTEKDATIASLEEtnrtltsDVANLANEKEELNNKLKDVQEQL 318
Cdd:TIGR02168 311 LANLERQLEELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEA-------ELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 319 SRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRgndtdvRRKEKENRKLHMELKSEREKLTQQmik 398
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK------KLEEAELKELQAELEELEEELEEL--- 452
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 109730369 399 yQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:TIGR02168 453 -QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
71-310 |
1.20e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 71 EAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQEnnhLM 150
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 151 EMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQL 230
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 231 EitltkadseqlarsIAEEQYSDLEKEKIMKEleikEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNK 310
Cdd:COG4942 181 A--------------ELEEERAALEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-421 |
1.77e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 24 KATKARLADKNKIYESIEEAKSEAMKEMEKKLLE-------ERTLKQKVENllLEAEKRcslldcDLKQSQQKINELLKQ 96
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREineisseLPELREELEK--LEKEVK------ELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 97 KDVLNEDVRNLTLKIeQETQKRC----LTQNDLKMQTQQVNTLKMSEKQ---LKQENNHLMEMKMNLEKQNAELRKERQD 169
Cdd:PRK03918 247 LESLEGSKRKLEEKI-RELEERIeelkKEIEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 170 ADGQMKELQDQleaeqyfstlyKTQVRELKEECEEKTKLGKELQQKKQELQDERdSLAAQLEITLTKADSEQLARSIAEE 249
Cdd:PRK03918 326 IEERIKELEEK-----------EERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 250 QYSDLEKEKIMKEL-EIKEMMARHKQELTEKDATIASLEET-------NRTLTSDvaNLANEKEELNNKLKDVQEQLSRL 321
Cdd:PRK03918 394 EELEKAKEEIEEEIsKITARIGELKKEIKELKKAIEELKKAkgkcpvcGRELTEE--HRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 322 KDEEISAAAIKAQFEKQLLTERTLKTQAvNKLAEIMNRKEPVKRGNDTDVRRKEKENRKlhmeLKSEREKLTQQMIKYQK 401
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLKKYNLEELEKKAEEYEK----LKEKLIKLKGEIKSLKK 546
|
410 420
....*....|....*....|
gi 109730369 402 ELNEMQAQIAEESQIRIELQ 421
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLD 566
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-364 |
1.80e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 59 RTLKQKVENLLLeaekrcSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKrcLTQNDLKMQ---------T 129
Cdd:TIGR02168 216 KELKAELRELEL------ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK--LEELRLEVSeleeeieelQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 130 QQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLG 209
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 210 KELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEmmARHKQELTEKDATIASLEET 289
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109730369 290 NRtltsdvanlanEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVK 364
Cdd:TIGR02168 446 EE-----------ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-441 |
4.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENL---LLEAEKRCSLLDCDLK 84
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 85 QSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELR 164
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 165 KERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLE----------ITL 234
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyegflegvkAAL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 235 TKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRtltSDVANLANEKEELNNKLKDV 314
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA---GRATFLPLDKIRARAALAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 315 QEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDV---------------RRKEKENR 379
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvtlegeggsaggsltGGSRRELL 671
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109730369 380 KLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-421 |
6.27e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKiyESIEEAKSEAmKEMEKKLLEertlKQKVENLLLEAEKRCSLLDCDLKQSQ 87
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAK--KKAEEDKKKA-DELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QKINELLKQKDVLNEDVRNLTLKIEQETQKrcltqNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLE--KQNAELRK 165
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKA-----DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 166 --ERQDADgQMKELQDQLEAEQYFSTLYKTQVRELKEECE-EKTKLGKELQQKKQELQDERDSL-AAQLEITLTKADSEQ 241
Cdd:PTZ00121 1518 aeEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEE 1596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 242 LARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVanlanEKEELNNKLKDVQEQLSRL 321
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-----KKAEEENKIKAAEEAKKAE 1671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 322 KDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSERE---KLTQQMIK 398
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEedkKKAEEAKK 1751
|
410 420
....*....|....*....|...
gi 109730369 399 YQKELNEMQAQIAEESQIRIELQ 421
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
8-441 |
7.63e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.36 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKarlaDKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSlldcdlKQSQ 87
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEK----EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ------GQME 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QKINELLKQKDVLnEDVRNLTLKIEQETQkrcLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKER 167
Cdd:pfam15921 448 RQMAAIQGKNESL-EKVSSLTAQLESTKE---MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 168 QDADGQMKELQdQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQEL-----QDERDSLAAQLEitltkadseql 242
Cdd:pfam15921 524 SRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgQHGRTAGAMQVE----------- 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 243 arsiaeeqYSDLEKEKIMKELEIKEMmarhKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQlsrlk 322
Cdd:pfam15921 592 --------KAQLEKEINDRRLELQEF----KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQE----- 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 323 deeisaaaikaqfEKQLLTERTLKTQAVNKLAEimnRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQmikyQKE 402
Cdd:pfam15921 655 -------------RDQLLNEVKTSRNELNSLSE---DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT----RNT 714
|
410 420 430
....*....|....*....|....*....|....*....
gi 109730369 403 LNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:pfam15921 715 LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL 753
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-441 |
1.03e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 166 ERQDADGQMKELQDQLEAEQYFSTLYKT-QVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTK-------- 236
Cdd:COG3206 62 EPQSSDVLLSGLSSLSASDSPLETQIEIlKSRPVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKgsnvieis 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 237 --ADSEQLARSIAE-------EQYSDLEKEKIMKELE-IKEMMARHKQELTEKDATIASLEETNrtltsDVANLANEKEE 306
Cdd:COG3206 142 ytSPDPELAAAVANalaeaylEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 307 LNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNklaeimnrkepvkrgnDTDVRRKEKENRKLHMELK 386
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------SPVIQQLRAQLAELEAELA 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 109730369 387 SEREKLTQQMIKYQkelnEMQAQIAE-ESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:COG3206 281 ELSARYTPNHPDVI----ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASL 332
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
44-406 |
1.20e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 44 KSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQK--INELLKQKDVLNEDVRNLTLKIEQETQKRCLT 121
Cdd:pfam02463 664 VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKeeLKKLKLEAEELLADRVQEAQDKINEELKLLKQ 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 122 QNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQyfstlyktQVRELKEE 201
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE--------EELKEEAE 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 202 CEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDA 281
Cdd:pfam02463 816 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 282 TIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEIS--AAAIKAQFEKQLLTERTLKTQAVNKLAEIMNR 359
Cdd:pfam02463 896 KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLleEADEKEKEENNKEEEEERNKRLLLAKEELGKV 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 109730369 360 KEPVKRgndtDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEM 406
Cdd:pfam02463 976 NLMAIE----EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| C1_Myosin-IX |
cd20818 |
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ... |
573-617 |
1.24e-08 |
|
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410368 Cd Length: 56 Bit Score: 51.53 E-value: 1.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 109730369 573 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 617
Cdd:cd20818 1 HNGHKFATVQFNIPTYCEVCNSFIWLMEK---GLVCQVCKFTCHK 42
|
|
| C1_p190RhoGEF-like |
cd20815 |
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ... |
574-630 |
1.79e-08 |
|
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide exchange factor (p190RhoGEF)-like family; The p190RhoGEF-like protein family includes p190RhoGEF, Rho guanine nucleotide exchange factor 2 (ARHGEF2), A-kinase anchor protein 13 (AKAP-13) and similar proteins. p190RhoGEF is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. ARHGEF2 acts as a guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. AKAP-13 is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. It activates RhoA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Members of this family share a common domain architecture containing C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains. Some members may contain additional domains such as the DUF5401 domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410365 Cd Length: 54 Bit Score: 50.88 E-value: 1.79e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109730369 574 KGHEFIPTLYHFPTNCEACMKPLwhmfKPPPALECRRCHIKCH----KDHmdkkeeiIAPC 630
Cdd:cd20815 2 NTHQFVPVSFSNSTKCDVCSKPL----TNKPALQCENCSVNVHdsscKDQ-------LADC 51
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-441 |
2.16e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLL---LEAEKRCSLLDCDLK 84
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALraaAELAAQLEELEEAEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 85 QSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNhlmemkmNLEKQNAELR 164
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-------LLEAALAELL 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 165 KERQDADGQMKELQDQLEAEQYFSTLYKTQVR-------------ELKEECEEKTKLGKELQQKKQELQDERDSLAAQLE 231
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLlaglrglagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAI 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 232 ITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNnKL 311
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV-TL 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 312 KDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEpvKRGNDTDVRRKEKENRKLHMELKSEREK 391
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--LELEEALLAEEEEERELAEAEEERLEEE 720
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 109730369 392 LTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSD---------IEQLRSQLQAL 441
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleelereLERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-324 |
2.49e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 14 QSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINEL 93
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 94 LKQKDVLNEDVRNLTLKIEQ-----ETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQ 168
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKleealNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 169 DADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAE 248
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 249 EQYSDLEKEKIMKELEIKEMMARHKQELTEKD---------ATIASLEETNRTLtSDVANLA-NEKEELNNKLKDVQEQL 318
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEeelsledvqAELQRVEEEIRAL-EPVNMLAiQEYEEVLKRLDELKEKR 995
|
....*.
gi 109730369 319 SRLKDE 324
Cdd:TIGR02169 996 AKLEEE 1001
|
|
| C1_PDZD8 |
cd20825 |
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ... |
573-622 |
3.06e-08 |
|
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410375 Cd Length: 55 Bit Score: 50.35 E-value: 3.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 109730369 573 HKGHEFIPTLYHFPTNCEACMKPLWHMFkpppALECRRCHIKCHKDHMDK 622
Cdd:cd20825 1 EGKHDFVLTQFQNATYCDFCKKKIWLKE----AFQCRLCGMICHKKCLDK 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-437 |
3.35e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMK---EMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLK 84
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 85 QSQQKINELLKQKDVLNEDVRNLTLKIEQETQKrcltQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELR 164
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK----ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 165 KERQDADGQMKELQDQLEAEQYFSTLYKT-----QVRELKEECEEKTKLGKELQQKKQELQD-------ERDSLAAQLEI 232
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeakKADEAKKKAEEAKKKADEAKKAAEAKKKadeakkaEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 233 TLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEElnnKLK 312
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE---EKK 1606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 313 DVQEQLSRLKDEEISAAAI-KAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSERE- 390
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEd 1686
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 109730369 391 --KLTQQMIKYQKE---LNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQ 437
Cdd:PTZ00121 1687 ekKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-314 |
4.49e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEeaksEAMKEMEKKLLEERTlkQKVENLLLEAEKRCSLLDCDLKQSQ 87
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLE----EALNDLEARLSHSRI--PEIQAELSKLEEEVSRIEARLREIE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QKINELLKQKDVLNEdvrnltlKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKER 167
Cdd:TIGR02169 819 QKLNRLTLEKEYLEK-------EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 168 QDADGQMKELQDQLEaeqyfstlyktqvrELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIA 247
Cdd:TIGR02169 892 DELEAQLRELERKIE--------------ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ 957
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109730369 248 EEQysdLEKEKIMKELEIKEMMArhKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDV 314
Cdd:TIGR02169 958 AEL---QRVEEEIRALEPVNMLA--IQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
35-414 |
5.35e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.52 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 35 KIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQE 114
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 115 TQKRCLT---QNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLY 191
Cdd:pfam02463 222 EEEYLLYldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 192 KTQVRELKEECEEKTKLGKELQQKKQElqderdslaaqleitltKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMAR 271
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEK-----------------ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 272 HKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVN 351
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109730369 352 KLAEimnrkepvkrGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEES 414
Cdd:pfam02463 445 KLTE----------EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-434 |
1.15e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 139 EKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEaeqyfstLYKTQVRELKEECEEKTKLGKELQQKKQE 218
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-------QLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 219 LQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKEL-EIKEMMARHKQELTEKDATIASLEETNRTLTSDV 297
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 298 ANLANEKEELNNKLKDVQEQLSRLKdeeISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVK--RGNDTDVRRKE 375
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRelERKIEELEAQI 912
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 109730369 376 KENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRiELQMTLDSKDSDIEQL 434
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-447 |
1.25e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 48 MKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKrclTQNDLKM 127
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEK---AKSLSKL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 128 QTQQVNTLKMSEKQLKQEnnhlmemkmnlEKQNAELRKERQDADGQMKELQDQLEAEQyfstlykTQVRELKeeceektk 207
Cdd:pfam01576 182 KNKHEAMISDLEERLKKE-----------EKGRQELEKAKRKLEGESTDLQEQIAELQ-------AQIAELR-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 208 lgKELQQKKQELQDerdslaaqleiTLTKADSEQLARSIAEEQYSDLEKE--KIMKELEiKEMMARHKQELTEKDatIAS 285
Cdd:pfam01576 236 --AQLAKKEEELQA-----------ALARLEEETAQKNNALKKIRELEAQisELQEDLE-SERAARNKAEKQRRD--LGE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 286 LEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAaaikaqFEKQLLTERTLKTQAVNKLAEIMNRKEPVKR 365
Cdd:pfam01576 300 ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRS------HEAQLQEMRQKHTQALEELTEQLEQAKRNKA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 366 GNDTDVRRKEKENRKLHMELKS----------EREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLR 435
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTlqqakqdsehKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
410
....*....|..
gi 109730369 436 SQLQALHIGLDS 447
Cdd:pfam01576 454 GKNIKLSKDVSS 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-493 |
1.61e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 247 AEEQYSDLEKEKImkelEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEI 326
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 327 SA----AAIKAQFEKQLlteRTL-KTQAVNKLAEIMNRKEPVK---------------RGNDTDVRRKEKENRKLHMELK 386
Cdd:COG4942 94 ELraelEAQKEELAELL---RALyRLGRQPPLALLLSPEDFLDavrrlqylkylaparREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 387 SEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHiGLDSSSIGSGPGDAEADDGFPES 466
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAAAERTPAAGFA 249
|
250 260
....*....|....*....|....*...
gi 109730369 467 RLEGWLSLPVRNN-TKKFGWVKKYVIVS 493
Cdd:COG4942 250 ALKGKLPWPVSGRvVRRFGERDGGGGRN 277
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-441 |
1.88e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 161 AELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLgKELQQKKQELqdERDSLAAQLEITLTKADSE 240
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY-QALLKEKREY--EGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 241 QLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDA----TIASLEETNRTLTSDVANLANEKEELNNKLKDVQE 316
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 317 QLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAE-------IMNRKEPVKRGNDTDVRRKEKENRKLHM------ 383
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAElkeeledLRAELEEVDKEFAETRDELKDYREKLEKlkrein 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 109730369 384 ELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
194-402 |
2.36e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 194 QVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIA--EEQYSDLEKEKimkeleikemmar 271
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAelEAELERLDASS------------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 272 hkQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERtlktqavn 351
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER-------- 754
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 109730369 352 klaeimnRKEPVKRGNDTDVRRK-EKENRKLHMELKSEREKLTQQMIKYQKE 402
Cdd:COG4913 755 -------FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| C1_1 |
pfam00130 |
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
576-618 |
4.20e-07 |
|
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.
Pssm-ID: 395079 Cd Length: 53 Bit Score: 47.05 E-value: 4.20e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHKD 618
Cdd:pfam00130 1 HHFVHRNFKQPTFCDHCGEFLWGLGKQ--GLKCSWCKLNVHKR 41
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
13-245 |
4.35e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 13 QQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKklLEERTlkQKVENLLLEAEKRCSLLDCDLKQSQQKINE 92
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--LERRI--AALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 93 LLK----QKDVLNEDVRNLTLKIEQETQKRCLTQND-------LKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNA 161
Cdd:COG4942 95 LRAeleaQKEELAELLRALYRLGRQPPLALLLSPEDfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 162 ELRKERQDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQ 241
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQ-------KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....
gi 109730369 242 LARS 245
Cdd:COG4942 248 FAAL 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-356 |
6.21e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 147 NHLME--MKMNLEKQNAELRKERQDADGQMKELQDQL-EAEQYFSTlYKTQ--VRELKEECEEKTKLGKELQQKKQELQD 221
Cdd:COG3206 155 NALAEayLEQNLELRREEARKALEFLEEQLPELRKELeEAEAALEE-FRQKngLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 222 ERDSLAAQLEI--TLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQE---LTEKDATIASLEETNRTLTSD 296
Cdd:COG3206 234 ELAEAEARLAAlrAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109730369 297 V-ANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQF---EKQLLTERTLKTQAVNKLAEI 356
Cdd:COG3206 314 IlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELrrlEREVEVARELYESLLQRLEEA 377
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
144-429 |
6.83e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 144 QENNHLME----MKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQEL 219
Cdd:pfam07888 41 QERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAE-------LKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 220 QDERDSLAAQleitltKADSEQLARSIaEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDAtiaslEETnrtltsdvan 299
Cdd:pfam07888 114 SEEKDALLAQ------RAAHEARIREL-EEDIKTLTQRVLERETELERMKERAKKAGAQRKE-----EEA---------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 300 lanEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLaeimnrkepvkrgndTDVRRKEKENR 379
Cdd:pfam07888 172 ---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---------------TTAHRKEAENE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 109730369 380 KLHMELKSEREKLT---QQMIKYQKELNEMQAQ----IAEESQIRIEL-QMTLDSKDS 429
Cdd:pfam07888 234 ALLEELRSLQERLNaseRKVEGLGEELSSMAAQrdrtQAELHQARLQAaQLTLQLADA 291
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
14-441 |
9.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 14 QSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEK--KLLEERTLKQKVENLLLEAEKRCSLLDcDLKQSQQKIN 91
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 92 ELLKQKDVLNEDVRNLTLKIEQETQKRCL-TQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDA 170
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 171 dgqmkELQDQLEAEQYFSTLYKTQVrelkeeceEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQ 250
Cdd:COG4717 240 -----ALEERLKEARLLLLIAAALL--------ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 251 YSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELnnKLKDVQEQLSRLkdeeisAAA 330
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAAL------LAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 331 IKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKlhmELKSEREKLTQQMIKYQKELNEMQAQI 410
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEELEEELEELREEL 455
|
410 420 430
....*....|....*....|....*....|...
gi 109730369 411 AE-ESQIR-IELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:COG4717 456 AElEAELEqLEEDGELAELLQELEELKAELREL 488
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
37-443 |
9.22e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 37 YESIEEAKSEAMKEMEKKL--LEERT--LKQKVENLLLEAEKRCSLLdcdLKQSQQKINELLKQKDVlneDVRNLTlkiE 112
Cdd:pfam15921 215 FRSLGSAISKILRELDTEIsyLKGRIfpVEDQLEALKSESQNKIELL---LQQHQDRIEQLISEHEV---EITGLT---E 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 113 QETQKRCLTQNdlkMQTQqvntLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYK 192
Cdd:pfam15921 286 KASSARSQANS---IQSQ----LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 193 TQVRELKEE-CEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADS--------EQLARSIAEEQYSDLEKEKIMKEL 263
Cdd:pfam15921 359 TEARTERDQfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitiDHLRRELDDRNMEVQRLEALLKAM 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 264 ------EIKEMMA--RHKQELTEKDATI-ASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQ 334
Cdd:pfam15921 439 ksecqgQMERQMAaiQGKNESLEKVSSLtAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 335 FEKqLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTdVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAE-E 413
Cdd:pfam15921 519 ITK-LRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQlE 596
|
410 420 430
....*....|....*....|....*....|....*.
gi 109730369 414 SQI---RIELQ---MTLDSKDSDIEQLRSQLQALHI 443
Cdd:pfam15921 597 KEIndrRLELQefkILKDKKDAKIRELEARVSDLEL 632
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
6-438 |
1.02e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 6 TYQLKVIQQSLEQEEAEHKATKARLADKNKIyeSIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQ 85
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLL--SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 86 SQQKINELLKQKDVLNEDVRNLTLKIEQETQKrcltqndLKMQTQQVNTLKMSEKQLKQE-----NNHLMEMKMNLEKQN 160
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK-------IKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 161 AELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSE 240
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 241 QLARSIAEEQYSDLEKEKIMKELEIKEMmarhKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSR 320
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERL----KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 321 LKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGND---TDVRRKEKENRKLHMELKSEREKLTQQMI 397
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEkleSEKKEKESKISDLEDELNKDDFELKKENL 559
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 109730369 398 K-----YQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQL 438
Cdd:TIGR04523 560 EkeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-441 |
1.21e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIE---EAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLK 84
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 85 QSQQKINELLKQKDVLNEDVRNLtlKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELR 164
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 165 KERQDADGQMKELQDQLEAeqyfstlyktqVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEIT--LTKADSEQL 242
Cdd:TIGR02168 475 QALDAAERELAQLQARLDS-----------LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegYEAAIEAAL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 243 ARSIAEEQYSDLEK-EKIMKELEIKEMMARHKQELT-EKDATIASLEETNRTLTSDVANLANEKEELNNKLKDV------ 314
Cdd:TIGR02168 544 GGRLQAVVVENLNAaKKAIAFLKQNELGRVTFLPLDsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllg 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 315 -----------QEQLSRLKDEE-------------------------------ISAAAIKAQFEKQLLTERTLKtQAVNK 352
Cdd:TIGR02168 624 gvlvvddldnaLELAKKLRPGYrivtldgdlvrpggvitggsaktnssilerrREIEELEEKIEELEEKIAELE-KALAE 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 353 LAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELK---SEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDS 429
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
490
....*....|..
gi 109730369 430 DIEQLRSQLQAL 441
Cdd:TIGR02168 783 EIEELEAQIEQL 794
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-337 |
1.27e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 131 QVNTLKMSEKQLKQENNHLMEmkmnLEKQNAELRKERQDADGQMKELQDQLEAEQyfsTLYKTQVRELKEECEEKTKLGK 210
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 211 ELQQKKQELQDERDSLAAQL------------EITLTKADSEQLARSIA-EEQYSDLEKEKIMKELEIKEMMARHKQELT 277
Cdd:COG4942 91 EIAELRAELEAQKEELAELLralyrlgrqpplALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109730369 278 EKDATIASLEETNRTLTSDVANLANEKEELNNKL-KDVQEQLSRLKDEEISAAAIKAQFEK 337
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
155-339 |
1.46e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 155 NLEKQNAELRKERQDADGQMKELQDQLEA--EQYFSTlyKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEI 232
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEElnEEYNEL--QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 233 TLTKADSEQL---ARSIAE--EQYSDLEKekIMKELeiKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEEL 307
Cdd:COG3883 98 SGGSVSYLDVllgSESFSDflDRLSALSK--IADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|..
gi 109730369 308 NNKLKDVQEQLSRLKDEEISAAAIKAQFEKQL 339
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
80-289 |
2.49e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 80 DCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKrcltQNDLKMQtqqvntLKMSEKQLKQENNHLMEMKMNLEKQ 159
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE----YNELQAE------LEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 160 NAELRKE-----RQDADGQM-------KELQDQLEAEQYFSTLYKTQ---VRELKEECEEKTKLGKELQQKKQELQDERD 224
Cdd:COG3883 85 REELGERaralyRSGGSVSYldvllgsESFSDFLDRLSALSKIADADadlLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109730369 225 SLAAQL-EITLTKADSEQLARSIAEEQySDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEET 289
Cdd:COG3883 165 ELEAAKaELEAQQAEQEALLAQLSAEE-AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-330 |
3.72e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 42 EAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELlkqkdvLNEDVRNLTLKIEQETQKRCLT 121
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 122 QNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQyfstlykTQVRELKEE 201
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR-------AELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 202 CEEKTKLGKELQQKKQELQDERDSLAAQLEitltkadseqlaRSIAEEQYSDLEKEKIMKELE-IKEMMARHKQELTEKD 280
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELD------------RLQEELQRLSEELADLNAAIAgIEAKINELEEEKEDKA 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 109730369 281 ATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAA 330
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
8-245 |
4.33e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAmkemekklleertlkqkvENLLLEAEKRCSLLDCDLKQSQ 87
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL------------------ARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QKINELLKQKDVLNEDVRNLTLKIEQETQKRCLtqnDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKER 167
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPL---ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 168 QDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSL---AAQLEITLTKADSEQLAR 244
Cdd:COG4942 167 AELEAERAELEALLAELE-------EERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAA 239
|
.
gi 109730369 245 S 245
Cdd:COG4942 240 A 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
24-440 |
6.88e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 24 KATKARLADKNKIYESI----------EEAKSEAMK---EMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKI 90
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEErkaeearkaeDAKKAEAVKkaeEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 91 NELLKQKDVLN-EDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQD 169
Cdd:PTZ00121 1275 EEARKADELKKaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 170 ADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKlGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSI--A 247
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkA 1433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 248 EEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRtlTSDVANLANEKEELNNKLKDVQEQLSRLKDEEIS 327
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 328 AAAIKAQFEKQLLTErtLKTQAVNKLAEIMNRKEPVKRGNDTdvrRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQ 407
Cdd:PTZ00121 1512 ADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKKKADEL---KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
410 420 430
....*....|....*....|....*....|...
gi 109730369 408 AQIaEESQIRIELQMTLDSKDSDIEQLRSQLQA 440
Cdd:PTZ00121 1587 KKA-EEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
17-324 |
7.36e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 17 EQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKrcslLDCDLKQSQQKINELLKQ 96
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE----KQRELEEKQNEIEKLKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 97 KDVLNEDVRNLT-------LKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQD 169
Cdd:TIGR04523 379 NQSYKQEIKNLEsqindleSKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 170 ADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEE 249
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 250 QYSDLEKEKI-----MKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE 324
Cdd:TIGR04523 539 KISDLEDELNkddfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
10-435 |
7.66e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 10 KVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLleaekRCSLLDCDLKQSQQK 89
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC-----GSQDEESDLERLKEE 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 90 INELLKQKDVLNEDVRNLTLKIEQETQKR--CLTQNDLKMQTqqvntlkmsEKQLKQENNHLMEMKMNLEKQNAELRKER 167
Cdd:TIGR00606 648 IEKSSKQRAMLAGATAVYSQFITQLTDENqsCCPVCQRVFQT---------EAELQEFISDLQSKLRLAPDKLKSTESEL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 168 QDADGQMKELQDQLEAEQyfsTLYKTQVRELKEECEEKTKLGKELQQKKQELQdERDSLAAQLEITLTKADSEQLARSIA 247
Cdd:TIGR00606 719 KKKEKRRDEMLGLAPGRQ---SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIM 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 248 EEQYSDLEK-EKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEI 326
Cdd:TIGR00606 795 ERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 327 S---AAAIKAQFEKQLLTERT-------LKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQ-- 394
Cdd:TIGR00606 875 QigtNLQRRQQFEEQLVELSTevqslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNih 954
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 109730369 395 ----------------QMIKYQKELNEMQAQIAE--ESQIRIELQMTLDSKDSDIEQLR 435
Cdd:TIGR00606 955 gymkdienkiqdgkddYLKQKETELNTVNAQLEEceKHQEKINEDMRLMRQDIDTQKIQ 1013
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-274 |
8.56e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEE-RTLKQKVENLLLE---AEKRCSLLDCDL 83
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEiasLERSIAEKEREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 84 KQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAEL 163
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 164 RKERQDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLA 243
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
250 260 270
....*....|....*....|....*....|.
gi 109730369 244 RSIAEEQYSDLEKEKIMKELEIKEMMARHKQ 274
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
13-439 |
8.79e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 13 QQSLEQEEAEHKATKARLADKNKIYESIEEAKS-EAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLL---DCDLKQSQQ 88
Cdd:TIGR00618 432 QQELQQRYAELCAAAITCTAQCEKLEKIHLQESaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELqeePCPLCGSCI 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 89 KINELLKQKDVLNEDVRNLtLKIEQETQKRCLTQNDLKMQTQQV-NTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKER 167
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRM-QRGEQTYAQLETSEEDVYHQLTSErKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 168 QDADGQMKELQDQLEAEQYFSTLYKTQVRELKEEcEEKTKLGKELQQKKQELQDERDSLaAQLEITLTKADSEQLARSIA 247
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE-QDLQDVRLHLQQCSQELALKLTAL-HALQLTLTQERVREHALSIR 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 248 --EEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLAN----EKEELNNKLKDVQEQLSRL 321
Cdd:TIGR00618 669 vlPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENasssLGSDLAAREDALNQSLKEL 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 322 KDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQK 401
Cdd:TIGR00618 749 MHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ 828
|
410 420 430
....*....|....*....|....*....|....*...
gi 109730369 402 ELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 439
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| C1_RASGRP |
cd20808 |
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ... |
576-631 |
1.12e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410358 Cd Length: 52 Bit Score: 43.09 E-value: 1.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHKDHmdkKEEIIAPCK 631
Cdd:cd20808 2 HNFQETTYFKPTFCDHCTGLLWGLIKQ--GYKCKDCGINCHKHC---KDLVVVECR 52
|
|
| C1_nPKC_theta-like_rpt1 |
cd20834 |
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
573-630 |
1.17e-05 |
|
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410384 Cd Length: 61 Bit Score: 43.47 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 109730369 573 HKGHEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMDKkeeIIAPC 630
Cdd:cd20834 5 VKGHEFIAKFFRQPTFCSVCKEFLWGFNK--QGYQCRQCNAAVHKKCHDK---ILGKC 57
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-437 |
2.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 18 QEEAEHKATKARLADKNKIYESIEEAKsEAMKEMEKKLLEErtLKQKVEnlllEAEKRcslldcdlKQSQQKINELLKQK 97
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADE--AKKKAE----EAKKA--------DEAKKKAEEAKKKA 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 98 DVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMemKMNLEKQNAELRKERQDADGQMKEL 177
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK--KKAEEKKKADEAKKKAEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 178 QDQLEAEqyfstlyKTQVRELKEECEEKTKlGKELQQKKQELQDERDSlaaqleitltKADSEQLARsiAEEQYSDLEKE 257
Cdd:PTZ00121 1410 LKKAAAA-------KKKADEAKKKAEEKKK-ADEAKKKAEEAKKADEA----------KKKAEEAKK--AEEAKKKAEEA 1469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 258 KIMKELEIKEMMARHKQELTEKdatiasLEETNRTltsdvANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEK 337
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKK------AEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 338 QLLTERTLKTQAVNKlAEIMNRKEPVKRGNDtdvRRKEKENRKLHM----ELKSEREKLTQQMIKYQKELNEM---QAQI 410
Cdd:PTZ00121 1539 AKKAEEKKKADELKK-AEELKKAEEKKKAEE---AKKAEEDKNMALrkaeEAKKAEEARIEEVMKLYEEEKKMkaeEAKK 1614
|
410 420
....*....|....*....|....*..
gi 109730369 411 AEESQIRIELQMTLDSKDSDIEQLRSQ 437
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
468-550 |
2.42e-05 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 43.69 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 468 LEGWLSlpVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFhVRPVTQTdvyraDAKEIPRIFQILY 547
Cdd:smart00233 3 KEGWLY--KKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCT-VREAPDP-----DSSKKPHCFEIKT 74
|
...
gi 109730369 548 ANE 550
Cdd:smart00233 75 SDR 77
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
249-446 |
2.77e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 249 EQYSDLEKEKImkELEIKEMMARHKQELTEK---DATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEE 325
Cdd:TIGR02169 211 ERYQALLKEKR--EYEGYELLKEKEALERQKeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 326 IsaAAIKAQFEKqLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMEL---KSEREKLTQQMIKYQKE 402
Cdd:TIGR02169 289 Q--LRVKEKIGE-LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIeeeRKRRDKLTEEYAELKEE 365
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 109730369 403 LNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLD 446
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-439 |
3.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 9 LKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVE---------NLLLEAEKRCSLL 79
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsefyEEYLDELREIEKR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 80 DCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQ------ETQKRCLTQNDLKMQTQQVNTLKMSEK-----QLKQENNH 148
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELYEEAKAKKEELERLKKRLTgltpeKLEKELEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 149 LMEMKMNLEKQNAELRKERQDADGQMKELQDQLEA----------------EQYFSTLYKTQVRELKEECEEKTKLGKEL 212
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 213 QQKKQELQDERDSLAAQLEITLTKADSEQLARsiAEEQYSDLEKEKIMKELEIKEMMarhKQELTEKDATIASLEETNRT 292
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKYNLEELEKKAEEYEKL---KEKLIKLKGEIKSLKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 293 LtsdvANLANEKEELNNKLKDVQEQLSRLKDEeisaaAIKAQFEKQLLTERTLKtqavnKLAEIMNRKEPVKrGNDTDVR 372
Cdd:PRK03918 551 L----EELKKKLAELEKKLDELEEELAELLKE-----LEELGFESVEELEERLK-----ELEPFYNEYLELK-DAEKELE 615
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109730369 373 RKEKENRKLHMELKSEREKLTQ---QMIKYQKELNEMQAQIAEESQIRI-----ELQMTLDSKDSDIEQLRSQLQ 439
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAEtekRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRRE 690
|
|
| C1_Myosin-IXa |
cd20883 |
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ... |
573-617 |
3.11e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410433 Cd Length: 58 Bit Score: 41.88 E-value: 3.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 109730369 573 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 617
Cdd:cd20883 3 HNGHIFKSTQYSIPTYCEYCSSLIWMMDR---AYVCKLCRYACHK 44
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
156-342 |
3.37e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 156 LEKQNAELRKERQDADGQMKELQDQLEAEQyfstlyktqvrelkeecEEKTKLGKELQQKKQELQDERDSLaaqleitlt 235
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAK-----------------TELEDLEKEIKRLELEIEEVEARI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 236 KADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQ 315
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|....*..
gi 109730369 316 EQLSRLKDEeisAAAIKAQFEKQLLTE 342
Cdd:COG1579 156 AELEELEAE---REELAAKIPPELLAL 179
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
148-442 |
3.82e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 148 HLMEMKMNLEkQNAELRKERQDAdgqmkelQDQLEAEQYfstLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLA 227
Cdd:PRK04863 277 HANERRVHLE-EALELRRELYTS-------RRQLAAEQY---RLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 228 AQLEITLTKADSEQL---------ARSIAEEQYSDLEKEKIMKELEIKEM---MARHKQ--ELTEKDA-----TIASLEE 288
Cdd:PRK04863 346 QQEKIERYQADLEELeerleeqneVVEEADEQQEENEARAEAAEEEVDELksqLADYQQalDVQQTRAiqyqqAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 289 TNRTLTSD---VANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEK----------------------QLLTE- 342
Cdd:PRK04863 426 AKQLCGLPdltADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagevsrseawdvarELLRRl 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 343 RTLKTQAV------NKLAEIMNRKEPVKRGNdtdvRRKEKENRKLHMELKSErEKLTQQMIKYQKELNEMQAQIAEESQI 416
Cdd:PRK04863 506 REQRHLAEqlqqlrMRLSELEQRLRQQQRAE----RLLAEFCKRLGKNLDDE-DELEQLQEELEARLESLSESVSEARER 580
|
330 340
....*....|....*....|....*.
gi 109730369 417 RIELQMTLDSKDSDIEQLRSQLQALH 442
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWL 606
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
275-447 |
3.99e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 275 ELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE------EISAAAIKAQFEKQLLTERTLKTQ 348
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklqaEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 349 ----AVNKLAEIMNRKEP---VKRGndTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQ 421
Cdd:COG3883 97 rsggSVSYLDVLLGSESFsdfLDRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*.
gi 109730369 422 MTLDSKDSDIEQLRSQLQALHIGLDS 447
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
19-245 |
4.25e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 19 EEAEHKATKA-RLADKNKIYESIEEAKSEAMKEMEKKLLEErtLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQK 97
Cdd:PRK05771 46 RKLRSLLTKLsEALDKLRSYLPKLNPLREEKKKVSVKSLEE--LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 98 DVLnEDVRNLTLKIEQETQKRCLTQ----------NDLKMQTQQVNTLKMSEKqlKQENNHLMemkMNLEKQNAELRKER 167
Cdd:PRK05771 124 ERL-EPWGNFDLDLSLLLGFKYVSVfvgtvpedklEELKLESDVENVEYISTD--KGYVYVVV---VVLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109730369 168 QDADGQMKELQDQLEAEQYFSTlYKTQVRELKEEceeKTKLGKELQQKKQELQDERDSLAAQLEITLTKAD-SEQLARS 245
Cdd:PRK05771 198 KKLGFERLELEEEGTPSELIRE-IKEELEEIEKE---RESLLEELKELAKKYLEELLALYEYLEIELERAEaLSKFLKT 272
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
62-315 |
5.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 62 KQKVENL---LLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNE---------DVRNLTLKIEQ-ETQKRCLTQN--DLK 126
Cdd:COG4913 609 RAKLAALeaeLAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAElEAELERLDASsdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 127 MQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDAD------GQMKELQDQLEAEQYFSTLYKTQVRElke 200
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAALGDAVER--- 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 201 eceektKLGKELQQKKQELQDERDSLAAQLEITLT------KADSEQLARSIAE-EQYsdlekEKIMKELEiKEMMARHK 273
Cdd:COG4913 766 ------ELRENLEERIDALRARLNRAEEELERAMRafnrewPAETADLDADLESlPEY-----LALLDRLE-EDGLPEYE 833
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 109730369 274 QELTE--KDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQ 315
Cdd:COG4913 834 ERFKEllNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
8-252 |
5.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQ 87
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QK------INELLKQKDVlnEDVrnltlkIEQETQKRCLTQNDLKMQTQQvntlkmseKQLKQEnnhLMEMKMNLEKQNA 161
Cdd:COG3883 97 RSggsvsyLDVLLGSESF--SDF------LDRLSALSKIADADADLLEEL--------KADKAE---LEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 162 ELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQ 241
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|.
gi 109730369 242 LARSIAEEQYS 252
Cdd:COG3883 238 AAAAAAASAAG 248
|
|
| C1_RASSF1-like |
cd20820 |
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ... |
575-616 |
5.18e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410370 Cd Length: 52 Bit Score: 41.27 E-value: 5.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 109730369 575 GHEFIPTLYHFPTNCEACMKPLWHMFkpPPALECRRCHIKCH 616
Cdd:cd20820 1 GHRFVPLELEQPTWCDLCGSVILGLF--RKCLRCANCKMTCH 40
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
29-357 |
5.52e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 29 RLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLT 108
Cdd:COG5185 216 GSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 109 LKIEQETQkrcltQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFS 188
Cdd:COG5185 296 EKIAEYTK-----SIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 189 TLYKTQvRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADS--EQLARSIAEEQYSDLEKEKIMKELEIK 266
Cdd:COG5185 371 ELSKSS-EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRqiEELQRQIEQATSSNEEVSKLLNELISE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 267 EMMARHKQELTEKDATIASLEETNRTLTSdvanlanEKEELNNKLKDVQEQLSRLKDEEisaAAIKAQFEKQLLTERTLK 346
Cdd:COG5185 450 LNKVMREADEESQSRLEEAYDEINRSVRS-------KKEDLNEELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKL 519
|
330
....*....|.
gi 109730369 347 TQAVNKLAEIM 357
Cdd:COG5185 520 DQVAESLKDFM 530
|
|
| C1_SpBZZ1-like |
cd20824 |
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ... |
576-616 |
6.27e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410374 Cd Length: 53 Bit Score: 41.15 E-value: 6.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCH 616
Cdd:cd20824 2 HNFKPHSFSIPTKCDYCGEKIWGLSK--KGLSCKDCGFNCH 40
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
182-421 |
7.23e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 182 EAEQYFSTLYK---TQVRELKEE-----CEEKTKLGKELQQKKQELQDERD--SLAAQLEITLTKADSEQLARSIAEEqY 251
Cdd:PRK05771 17 YKDEVLEALHElgvVHIEDLKEElsnerLRKLRSLLTKLSEALDKLRSYLPklNPLREEKKKVSVKSLEELIKDVEEE-L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 252 SDLEKE--KIMKEL-EIKEMMARHKQELTE----KDATIA-SLEETNRTLTSDVANLANEKEELNNKLKD--VQEQLSRL 321
Cdd:PRK05771 96 EKIEKEikELEEEIsELENEIKELEQEIERlepwGNFDLDlSLLLGFKYVSVFVGTVPEDKLEELKLESDveNVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 322 KDEEISAAAIKAQFEKQLLTErtlktqavnkLAEIMNRKEPVKRGNDTDVRRKEKENRKlhMELKSEREKLTQQMIKYQK 401
Cdd:PRK05771 176 KGYVYVVVVVLKELSDEVEEE----------LKKLGFERLELEEEGTPSELIREIKEEL--EEIEKERESLLEELKELAK 243
|
250 260
....*....|....*....|
gi 109730369 402 ELNEMQAQIAEESQIRIELQ 421
Cdd:PRK05771 244 KYLEELLALYEYLEIELERA 263
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
8-322 |
7.47e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLleerTLKQKVENLLLEAEKRCSLLDCDLKQSQ 87
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI----RLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QKINELLKQKDVLNEDVRNLTLKIEQETQ--KRCLTQNDLKMQTQQvntlkmSEKQLKQENNHLMEMKM-NLEKQNAELR 164
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSelRRQIQRAELELQSTN------SELEELQERLDLLKAKAsEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 165 ---KERQDADGQMKELQDQLEAEQYFSTLYKTqvreLKEECEEKTKLGKELQQKKQ------ELQDERDSLAAQLEITLT 235
Cdd:pfam05557 160 kqqSSLAEAEQRIKELEFEIQSQEQDSEIVKN----SKSELARIPELEKELERLREhnkhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 236 KADSEQLARsiAEEQYSDLEKEKIMKEL----------------------EIKEMMAR---HKQELTEKDATIASLEETN 290
Cdd:pfam05557 236 KLEREEKYR--EEAATLELEKEKLEQELqswvklaqdtglnlrspedlsrRIEQLQQReivLKEENSSLTSSARQLEKAR 313
|
330 340 350
....*....|....*....|....*....|..
gi 109730369 291 RTLTSDVANLANEKEELNNKLKDVQEQLSRLK 322
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQ 345
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
13-441 |
8.48e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 13 QQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKvenlLLEAEKRCSLLDCDLKQSQQKINE 92
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQQRYAELCAAAITC 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 93 LLKQKDVLNEDVRNLTLKIEQETQKrcltQNDLKMQTQQVNTLKMSEKQLKQEnnhLMEMKMNLEKQNAELRKERQDADg 172
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQ----LQTKEQIHLQETRKKAVVLARLLE---LQEEPCPLCGSCIHPNPARQDID- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 173 QMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQleITLTKADSEQLarsiaeEQYS 252
Cdd:TIGR00618 522 NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC--DNRSKEDIPNL------QNIT 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 253 DLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNnklkdvQEQLSRLKDEEISAAAIK 332
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH------ALQLTLTQERVREHALSI 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 333 AQFEKQLLTERTLKTQAVNKLA-------EIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNE 405
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKeqltywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
410 420 430
....*....|....*....|....*....|....*.
gi 109730369 406 MQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
159-437 |
9.19e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 159 QNAELRKERQDADGQMKELQDQLEAeqyfstlyktQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKAD 238
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVE----------MARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 239 SEQL---------ARSIAEEQYSDLEKEKIMKELEIKEM---MARHKQELTEKDA-------TIASLEETNRTLTSD--- 296
Cdd:COG3096 356 LEELterleeqeeVVEEAAEQLAEAEARLEAAEEEVDSLksqLADYQQALDVQQTraiqyqqAVQALEKARALCGLPdlt 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 297 VANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEK----------------------QLLTE-RTLKTQAVN-- 351
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiageversqawqtarELLRRyRSQQALAQRlq 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 352 ----KLAEIMNRKEpvkrgNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSK 427
Cdd:COG3096 516 qlraQLAELEQRLR-----QQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL 590
|
330
....*....|
gi 109730369 428 DSDIEQLRSQ 437
Cdd:COG3096 591 RARIKELAAR 600
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
12-439 |
9.43e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 12 IQQSLE------QEEAEHKATKARLADKNKIYESIEEAKSEaMKEMEKKLLE-ERTLKQKVENLL-----LEAEKRCSLL 79
Cdd:PRK11281 41 VQAQLDalnkqkLLEAEDKLVQQDLEQTLALLDKIDRQKEE-TEQLKQQLAQaPAKLRQAQAELEalkddNDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 80 DCDLKQSQQKINELLKQKDVLNEDVRNL-TLKIEQETQ----KRCLTQNdlKMQTQQVNTLKMSEKQLKQENNHLMEMKM 154
Cdd:PRK11281 120 TLSLRQLESRLAQTLDQLQNAQNDLAEYnSQLVSLQTQperaQAALYAN--SQRLQQIRNLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 155 N-----LEKQNAELRKERQDADgqmkELQDqleaeqyfstLYKTQvRELKEECEEKtklgkeLQQKKQELQDE-RDSLAA 228
Cdd:PRK11281 198 QaeqalLNAQNDLQRKSLEGNT----QLQD----------LLQKQ-RDYLTARIQR------LEHQLQLLQEAiNSKRLT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 229 QLEITLTKADSEQLARSIaeeQYSDLekekIMKELEIkemmarhKQELTEKdaTIASLEETNrTLTSDvaNLANeKEELN 308
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARI---QANPL----VAQELEI-------NLQLSQR--LLKATEKLN-TLTQQ--NLRV-KNWLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 309 NKLkdvqeQLSRLKDEEISA-------AAIKAQfEKQLLTERTLKTQAVNKLA-------EIMNRKEPVKRGND--TDVR 372
Cdd:PRK11281 317 RLT-----QSERNIKEQISVlkgslllSRILYQ-QQQALPSADLIEGLADRIAdlrleqfEINQQRDALFQPDAyiDKLE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109730369 373 RKEKE--NRKLHMELKS---EREKLTQQMIkyqKELNemqAQIAEEsqirIELQMTLDSKDSDIEQLRSQLQ 439
Cdd:PRK11281 391 AGHKSevTDEVRDALLQlldERRELLDQLN---KQLN---NQLNLA----INLQLNQQQLLSVSDSLQSTLT 452
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
9-439 |
1.31e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 9 LKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKrcslLDCDLKQSQQ 88
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK----AEKELKKEKE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 89 KINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLK--MQTQQVNTlKMSEKQLKQENNHLMEMKMNLEKQNAELRKE 166
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEelLAKKKLES-ERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 167 RQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSI 246
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 247 AEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLtsDVANLANEKEELNNKLKDVQEQLSRLKDEE- 325
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY--KVAISTAVIVEVSATADEVEERQKLVRALTe 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 326 --ISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKEL 403
Cdd:pfam02463 573 lpLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
410 420 430
....*....|....*....|....*....|....*.
gi 109730369 404 NEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 439
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
19-403 |
1.31e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 19 EEAEHKATKARLADKNKI---YESIEEAKSEAMKEMEKK----------LLEERTLKQKVENLLLEAEKRCSLLDCDLKQ 85
Cdd:pfam05483 200 EELRVQAENARLEMHFKLkedHEKIQHLEEEYKKEINDKekqvsllliqITEKENKMKDLTFLLEESRDKANQLEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 86 SQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNH--------LMEMKMNLE 157
Cdd:pfam05483 280 QDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvVTEFEATTC 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 158 KQNAELRKERQDADGQMKELQ----------DQLEAEQYFSTLYKTQVRELKEECEEKT----------KLGKELQQKKQ 217
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEDQLKiitmelqkksSELEEMTKFKNNKEVELEELKKILAEDEklldekkqfeKIAEELKGKEQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 218 ELQ---DERDSLAAQLEITLTK-ADSEQLARSIAEEQYSDLEKEKI----------MKELEIKEMMARHKQ---ELTEKD 280
Cdd:pfam05483 440 ELIfllQAREKEIHDLEIQLTAiKTSEEHYLKEVEDLKTELEKEKLknieltahcdKLLLENKELTQEASDmtlELKKHQ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 281 ATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE--------EISAAAIKAQFEKQLLTERTLKTQAVNK 352
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkckldksEENARSIEYEVLKKEKQMKILENKCNNL 599
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109730369 353 LAEIMNRK---EPVKRGNDTDVRRKEKENR----------KLHMELKSEREKLTQQMIKYQKEL 403
Cdd:pfam05483 600 KKQIENKNkniEELHQENKALKKKGSAENKqlnayeikvnKLELELASAKQKFEEIIDNYQKEI 663
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
9-439 |
1.48e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 9 LKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEME--KKLLEErtlkqkvENLLLEAEKRCSLLDCDLKQS 86
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelKKILAE-------DEKLLDEKKQFEKIAEELKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 87 QQKINELLKQKDvlnEDVRNLTLKIEqetqkrcLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKE 166
Cdd:pfam05483 438 EQELIFLLQARE---KEIHDLEIQLT-------AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 167 RQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEEceeKTKLGKELQQKKQELQDERDSLAAQLEitltkaDSEQLARSI 246
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK---EMNLRDELESVREEFIQKGDEVKCKLD------KSEENARSI 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 247 aeeQYSDLEKEKIMKELEIKemMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKD--E 324
Cdd:pfam05483 579 ---EYEVLKKEKQMKILENK--CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfE 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 325 EISAAAIKAQFEKQLLTERTLktQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMikyQKELN 404
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLL--EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELG 728
|
410 420 430
....*....|....*....|....*....|....*
gi 109730369 405 EMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 439
Cdd:pfam05483 729 LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLE 763
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-460 |
1.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 19 EEAEHKATKARLADK-NKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQK 97
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 98 DVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLK-QENNHLMEMKMNLEKQNAELRKERQDADGQMKE 176
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 177 LQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEK 256
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 257 EKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANE--KEELNNKLKdvQEQLSRLKDEEISAAAIKAQ 334
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkKAEEENKIK--AEEAKKEAEEDKKKAEEAKK 1751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 335 FEKQLLTERTLKTQAVNKLAEIMNRKEPVKRgndtDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEES 414
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM 1827
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 109730369 415 QIRiELQMTLDSKDSDIEQLRSQLQAlhiGLDSSSIGSGPGDAEAD 460
Cdd:PTZ00121 1828 EDS-AIKEVADSKNMQLEEADAFEKH---KFNKNNENGEDGNKEAD 1869
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
4-409 |
1.65e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 4 DMTYQLKVIQQSLEQEEAEHKATKARL----ADKNKIYESIEEAKSEaMKEMEKKLLEERTLKQKVENLLLEAEKRCSLL 79
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLeeetAQKNNALKKIRELEAQ-ISELQEDLESERAARNKAEKQRRDLGEELEAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 80 DCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKM-QTQQVNTLKMSEKQLKQennhlmeMKMNLEK 158
Cdd:pfam01576 305 KTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkHTQALEELTEQLEQAKR-------NKANLEK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 159 QNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKAD 238
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 239 SEQLARSIAEEQYSDLEkekimkelEIKEMMARHKQELTEKdatIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQL 318
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQ--------ELLQEETRQKLNLSTR---LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 319 SRLK---DEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKrgndtdvRRKEKENRKLHMELKSEREkLTQQ 395
Cdd:pfam01576 527 SDMKkklEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTK-------NRLQQELDDLLVDLDHQRQ-LVSN 598
|
410
....*....|....
gi 109730369 396 MIKYQKELNEMQAQ 409
Cdd:pfam01576 599 LEKKQKKFDQMLAE 612
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
61-246 |
2.46e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 61 LKQKVENLLLEAEKRCSLLdcdLKQSQQKINELLKQKDV-LNEDVRNLTLKIEQETQKRcltQNDLKMQtqqvntlkmsE 139
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRI---LEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKL----------E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 140 KQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELqDQLEAEqyfstlYKTQVRELKEECEEKTKLGKE------LQ 213
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL-EKKEEE------LEELIEEQLQELERISGLTAEeakeilLE 161
|
170 180 190
....*....|....*....|....*....|...
gi 109730369 214 QKKQELQDERDSLAAQLEiTLTKADSEQLARSI 246
Cdd:PRK12704 162 KVEEEARHEAAVLIKEIE-EEAKEEADKKAKEI 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
56-322 |
2.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 56 LEERTLKQKVENLLleaekrcSLLDcDLKQSQQKINELLKQKDVLnEDVRNLTLKIEQETQkrcltqnDLKMQTQQVNTL 135
Cdd:COG4913 218 LEEPDTFEAADALV-------EHFD-DLERAHEALEDAREQIELL-EPIRELAERYAAARE-------RLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 136 KMSEKQLKQENnhlmemkmnLEKQNAELRKERQDADGQMKELQDQLEAEQyfstlykTQVRELKEEC-----EEKTKLGK 210
Cdd:COG4913 282 RLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALR-------EELDELEAQIrgnggDRLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 211 ELQQKKQELqDERDSLAAQLeitltkadsEQLARSIAEEQYSDLEkekimkelEIKEMMARHKQELTEKDATIASLEEtn 290
Cdd:COG4913 346 EIERLEREL-EERERRRARL---------EALLAALGLPLPASAE--------EFAALRAEAAALLEALEEELEALEE-- 405
|
250 260 270
....*....|....*....|....*....|..
gi 109730369 291 rtltsDVANLANEKEELNNKLKDVQEQLSRLK 322
Cdd:COG4913 406 -----ALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-442 |
2.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 83 LKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEK--QN 160
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 161 AELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAA----QLEITLTK 236
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 237 ADSEQLARSIAEEQYSDLE-----KEKIMKELEIKEMMARHKQELTEKD------ATIASLEETNRTLTSDVANLA---- 301
Cdd:COG4717 201 LEELQQRLAELEEELEEAQeeleeLEEELEQLENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAgvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 302 --------------NEKEELNNKLKDVQ--EQLSRLKDEEISAAAIKAQFEKQLLTERTLK-----TQAVNKLAEIMNRK 360
Cdd:COG4717 281 lvlgllallflllaREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLElldriEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 361 EPVKR----------------GNDTDVRRKEKENRKLHmELKSEREKLTQQMIKYQKELNEMQAQIAEES-QIRI-ELQM 422
Cdd:COG4717 361 EELQLeeleqeiaallaeagvEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEElEEELeELEE 439
|
410 420
....*....|....*....|
gi 109730369 423 TLDSKDSDIEQLRSQLQALH 442
Cdd:COG4717 440 ELEELEEELEELREELAELE 459
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
34-436 |
2.88e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 34 NKIYESIEEAKsEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCdlkqsQQKINELLKQKDVlNEDVRNLTLKIEQ 113
Cdd:TIGR01612 1358 NKIKKIIDEVK-EYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEEC-----KSKIESTLDDKDI-DECIKKIKELKNH 1430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 114 ETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMkMNLEKQNAElrkerQDADGQMKELQDQLEAeqyfSTLYKT 193
Cdd:TIGR01612 1431 ILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHI-LKIKKDNAT-----NDHDFNINELKEHIDK----SKGCKD 1500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 194 QVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIaeeqySDLEKEKIMKELEIKEMMARHK 273
Cdd:TIGR01612 1501 EADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEI-----KDAHKKFILEAEKSEQKIKEIK 1575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 274 QELTEKDATIASLEETNRT---LTSDVANLANEKEELNNKLKDVQEQLSRLK--DEEISAAAIKAQfekqlLTERTLKTQ 348
Cdd:TIGR01612 1576 KEKFRIEDDAAKNDKSNKAaidIQLSLENFENKFLKISDIKKKINDCLKETEsiEKKISSFSIDSQ-----DTELKENGD 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 349 AVNKLAEIMNRKEPVKRgndtDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIElqMTLDSKD 428
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKK----NIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIE--SIKELIE 1724
|
....*...
gi 109730369 429 SDIEQLRS 436
Cdd:TIGR01612 1725 PTIENLIS 1732
|
|
| C1_RASSF1 |
cd20885 |
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ... |
573-616 |
2.93e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410435 Cd Length: 54 Bit Score: 39.17 E-value: 2.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 109730369 573 HKGHEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCH 616
Cdd:cd20885 1 GEGHDFQPCSLTNPTWCDLCGDFIWGLYKQ--CLRCTHCKYTCH 42
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6-409 |
3.49e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 6 TYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEkrcslldcDLKQ 85
Cdd:TIGR00618 271 ELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS--------SIEE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 86 SQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNdLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRK 165
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH-IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 166 ERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERdslaaqlEITLTKADSEQLARS 245
Cdd:TIGR00618 422 LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE-------QIHLQETRKKAVVLA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 246 IAEEQYsdlEKEKIMKELEIKEMMARHKQELTEKDAT-IASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE 324
Cdd:TIGR00618 495 RLLELQ---EEPCPLCGSCIHPNPARQDIDNPGPLTRrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 325 eisaaaikaqfEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDtdvrrkeKENRKLHMELKSEREKLTQQMIKYQKELN 404
Cdd:TIGR00618 572 -----------FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS-------EAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
....*
gi 109730369 405 EMQAQ 409
Cdd:TIGR00618 634 LQQCS 638
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
8-166 |
3.85e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.88 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQqSLEQEEAEHKATKARLADKnkiYESIEEAKSEAMKEMEKKLleeRTLKQKVENLLlEAEKrcslldcDLKQSQ 87
Cdd:pfam10168 573 QLQELQ-SLEEERKSLSERAEKLAEK---YEEIKDKQEKLMRRCKKVL---QRLNSQLPVLS-DAER-------EMKKEL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QKINELLKQKDVlnedvRNLTLKIEQETQKRCLTQNdlkMQTQQVNTLKMSEKQLKQENNHLMEMK---MNLEKQNAELR 164
Cdd:pfam10168 638 ETINEQLKHLAN-----AIKQAKKKMNYQRYQIAKS---QSIRKKSSLSLSEKQRKTIKEILKQLGseiDELIKQVKDIN 709
|
..
gi 109730369 165 KE 166
Cdd:pfam10168 710 KH 711
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
191-438 |
4.63e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 191 YKTQVRELKEECEEKTKLGK-----------ELQQKKQELQDERDSLAaqlEITLTKADSEQLARSIAEEQYSDLEKEKI 259
Cdd:pfam15921 83 YSHQVKDLQRRLNESNELHEkqkfylrqsviDLQTKLQEMQMERDAMA---DIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 260 MKE----------LEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLA-----NEKEELNNKLKDVQEQLSRLK-- 322
Cdd:pfam15921 160 LKEdmledsntqiEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMStmhfrSLGSAISKILRELDTEISYLKgr 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 323 ----DEEISAAAIKAQFEKQLLTErtlktQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIK 398
Cdd:pfam15921 240 ifpvEDQLEALKSESQNKIELLLQ-----QHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM 314
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 109730369 399 YQKELNEMQAQIaeeSQIRIELQMTLDSKDSDIEQLRSQL 438
Cdd:pfam15921 315 YMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQL 351
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
8-361 |
4.71e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLlEAEKRCSLLDCDLKQsQ 87
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAE-K 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 88 QKINELLKQKdvlnedVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLK----QENNHLMEMKMNLEKQNAEL 163
Cdd:pfam15921 561 DKVIEILRQQ------IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdKKDAKIRELEARVSDLELEK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 164 RK------ERQDADGQMKELQDQLEAEqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITltKA 237
Cdd:pfam15921 635 VKlvnagsERLRAVKDIKQERDQLLNE------VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA--QS 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 238 DSEQLARSIAEEQYSDLEKEKIMKELEiKEMMARHKQ--------ELTEKDATIAS-----LEETNRTLTSDVANLANEK 304
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQ-KQITAKRGQidalqskiQFLEEAMTNANkekhfLKEEKNKLSQELSTVATEK 785
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109730369 305 EELNNKLKDVQEQLSRLKDE----EISAAAIKAQF-EKQLLTERTLKTQAVNKLAEIMNRKE 361
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKvanmEVALDKASLQFaECQDIIQRQEQESVRLKLQHTLDVKE 847
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
149-236 |
4.92e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 149 LMEMKMNLEKQNAELRKERQDADGQMKELQDQLEA-EQYFSTLYKTQ-------VRELKEECEEKTKLGKELQ------Q 214
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAekeaqqaIKEAKKEADEIIKELRQLQkggyasV 604
|
90 100
....*....|....*....|..
gi 109730369 215 KKQELQDERDSLAAQLEITLTK 236
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKK 626
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
71-439 |
5.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 71 EAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLM 150
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 151 EMKMNLEKQNAELRKERQDADGQMKelqdqleaeqyfstLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQL 230
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNID--------------KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 231 EITLTKADSEQLARSIAEEQYSDLEKekimkeleikemmarHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNK 310
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKK---------------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 311 LKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKrgndtdvrrKEKENrKLHMELKSERE 390
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN---------NQKEQ-DWNKELKSELK 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 109730369 391 KLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 439
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
56-441 |
6.80e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 56 LEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKmqtQQVNTL 135
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELE---SRVAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 136 KMSEKQLKQENNHLMEMKMNLEKQNAELRKER-------QDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKL 208
Cdd:pfam07888 86 KEELRQSREKHEELEEKYKELSASSEELSEEKdallaqrAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 209 GKELQQKKQELQDERDslAAQLEITLTKADSEQLARSIAeeqysdlekEKIMKELEIKEMMARHKQELTEKDATIASLEE 288
Cdd:pfam07888 166 RKEEEAERKQLQAKLQ--QTEEELRSLSKEFQELRNSLA---------QRDTQVLQLQDTITTLTQKLTTAHRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 289 TNRTLTSdvanlanekeeLNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEiMNRKEPVKRGNd 368
Cdd:pfam07888 235 LLEELRS-----------LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAD-ASLALREGRAR- 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109730369 369 tdvRRKEKENRKLHMELKSER-EKLTQQMIKYQKELnemQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:pfam07888 302 ---WAQERETLQQSAEADKDRiEKLSAELQRLEERL---QEERMEREKLEVELGREKDCNRVQLSESRRELQEL 369
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
237-358 |
7.21e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 237 ADSEQLARSIAEEQYSDLEKEKIMKELEIKEMM----ARHKQELTEKDATIASLEETnrtltsdvanLANEKEELNNKLK 312
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIhklrNEFEKELRERRNELQKLEKR----------LLQKEENLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 109730369 313 DVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMN 358
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG 149
|
|
| C1_cPKC_nPKC_rpt1 |
cd20792 |
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ... |
575-617 |
7.79e-04 |
|
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410342 Cd Length: 53 Bit Score: 37.99 E-value: 7.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 109730369 575 GHEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHK 617
Cdd:cd20792 1 GHKFVATFFKQPTFCSHCKDFIWGLGKQ--GYQCQVCRFVVHK 41
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-441 |
8.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 19 EEAEHKATKAR-----LADKNKIYESIEEAKSEAMkemEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINEL 93
Cdd:COG4913 238 ERAHEALEDAReqielLEPIRELAERYAAARERLA---ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 94 LKQKDVLNEDVRNLTLKIEQETQKRcLTQ--NDLKMQTQQVNTLKMSEKQLKQENNHLmEMKMNLEKQN-AELRKERQDA 170
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR-LEQleREIERLERELEERERRRARLEALLAAL-GLPLPASAEEfAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 171 DGQMKELQDQLEAEQYFStlyKTQVRELKEECEEKTKLGKELQQKK----QELQDERDSLAAQLEITLT----------- 235
Cdd:COG4913 393 LEALEEELEALEEALAEA---EAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALGLDEAelpfvgeliev 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 236 KADSEQ-----------LARSI--AEEQYSDLEK-------------EKIMKELEIKEMMARHKQELTEK---------- 279
Cdd:COG4913 470 RPEEERwrgaiervlggFALTLlvPPEHYAAALRwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkphpfra 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 280 ----------D----ATIASLEETNRTLTSD-------------------------------VANLANEKEELNNKLKDV 314
Cdd:COG4913 550 wleaelgrrfDyvcvDSPEELRRHPRAITRAgqvkgngtrhekddrrrirsryvlgfdnrakLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 315 QEQLSRLKDEEISAAAIKAQFEK-QLLTERTLKT-QAVNKLAEIMNRKEPVKRGNDtDVRrkekenrklhmELKSEREKL 392
Cdd:COG4913 630 EERLEALEAELDALQERREALQRlAEYSWDEIDVaSAEREIAELEAELERLDASSD-DLA-----------ALEEQLEEL 697
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 109730369 393 tqqmikyQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 441
Cdd:COG4913 698 -------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| C1_dGM13116p-like |
cd20831 |
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ... |
573-617 |
8.59e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410381 Cd Length: 58 Bit Score: 38.09 E-value: 8.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 109730369 573 HKGHEFIPTlyHF--PTNCEACMKPLWHMF-KPppALECRRCHIKCHK 617
Cdd:cd20831 3 YNDHTFVAT--HFkgGPSCAVCNKLIPGRFgKQ--GYQCRDCGLICHK 46
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
222-390 |
8.65e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 222 ERDSLAAQLEITLTKADS-EQLARSIAEeqYSDLEKEKI--------------MKELEIKEMMARHKQELTEKDATIASL 286
Cdd:COG2433 334 ERDALAAALKAYDAYKNKfERVEKKVPP--DVDRDEVKArvirglsieealeeLIEKELPEEEPEAEREKEHEERELTEE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 287 EETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEeisaaaikAQFEKQLLTERTLKTQAVNKLAEIMNRKEpvkrg 366
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE--------LSEARSEERREIRKDREISRLDREIERLE----- 478
|
170 180
....*....|....*....|....
gi 109730369 367 ndTDVRRKEKENRKLHMELKSERE 390
Cdd:COG2433 479 --RELEEERERIEELKRKLERLKE 500
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
253-443 |
9.08e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 253 DLEKEKI-MKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAI 331
Cdd:PHA02562 191 DHIQQQIkTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 332 KAQFEK--QLLTERTL---KTQAVNKLAEIMnrkepvkrgndTDVRRKEKENRKLHMELKSEREKLTQQMIKY---QKEL 403
Cdd:PHA02562 271 IEQFQKviKMYEKGGVcptCTQQISEGPDRI-----------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqSKKL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 109730369 404 NEMQAQIAEESQIRIelqmTLDSKDSDIEQLRSQLQALHI 443
Cdd:PHA02562 340 LELKNKISTNKQSLI----TLVDKAKKVKAAIEELQAEFV 375
|
|
| C1_MTMR-like |
cd20828 |
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ... |
576-616 |
9.40e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410378 Cd Length: 57 Bit Score: 37.81 E-value: 9.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCH 616
Cdd:cd20828 6 HNFEPHSFVTPTNCDYCLQILWGIVK--KGMKCSECGYNCH 44
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
12-440 |
1.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 12 IQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMeKKLLEERTLKQKVENLLLEAEKRCSLLDCD---LKQSQQ 88
Cdd:PRK01156 202 IKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL-NELSSLEDMKNRYESEIKTAESDLSMELEKnnyYKELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 89 KINELLKQKDVLNEDVRN--LTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKM-NLEKQNAELRK 165
Cdd:PRK01156 281 RHMKIINDPVYKNRNYINdyFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYdDLNNQILELEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 166 ERQDADGQMKELQ-----------DQLEAEQYFSTLYKTQV---RELKEECEE--------KTKLGKeLQQKKQELQDER 223
Cdd:PRK01156 361 YEMDYNSYLKSIEslkkkieeyskNIERMSAFISEILKIQEidpDAIKKELNEinvklqdiSSKVSS-LNQRIRALRENL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 224 DSLAAQLEI------------TLTKADSEQLARSIAEEQySDLEKEKIMKELEIKEMMARHKQELTEKDaTIASlEETNR 291
Cdd:PRK01156 440 DELSRNMEMlngqsvcpvcgtTLGEEKSNHIINHYNEKK-SRLEEKIREIEIEVKDIDEKIVDLKKRKE-YLES-EEINK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 292 TLTSDvanlaNEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFE--------------------KQLLTERTLKTQ--- 348
Cdd:PRK01156 517 SINEY-----NKIESARADLEDIKIKINELKDKHDKYEEIKNRYKslkledldskrtswlnalavISLIDIETNRSRsne 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 349 -------AVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLH------MELKSEREKLTQQMIKYQKELNEMQAQIAEESQ 415
Cdd:PRK01156 592 ikkqlndLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNnkyneiQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE 671
|
490 500
....*....|....*....|....*
gi 109730369 416 IRIELqmtLDSKDsDIEQLRSQLQA 440
Cdd:PRK01156 672 ITSRI---NDIED-NLKKSRKALDD 692
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
469-554 |
1.10e-03 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 39.08 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 469 EGWLSlpVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKlfhvrpVTQTDVYRADAKEIPRIFQILYA 548
Cdd:pfam00169 4 EGWLL--KKGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSG------CEVVEVVASDSPKRKFCFELRTG 75
|
....*.
gi 109730369 549 NEGESK 554
Cdd:pfam00169 76 ERTGKR 81
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
190-355 |
1.15e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.35 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 190 LYKTQVRELKEECE----EKTKLGKELQQKKQELQderdSLAAQLEitltkaDSEQLARSIaEEQYSDLEKEKIMKELEI 265
Cdd:pfam05911 678 LKTEENKRLKEEFEqlksEKENLEVELASCTENLE----STKSQLQ------ESEQLIAEL-RSELASLKESNSLAETQL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 266 KEMMARHKQ---ELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIkAQFEKQLLTE 342
Cdd:pfam05911 747 KCMAESYEDletRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDA-DQEDKKLQQE 825
|
170
....*....|...
gi 109730369 343 RTLkTQAVNKLAE 355
Cdd:pfam05911 826 KEI-TAASEKLAE 837
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
9-246 |
1.17e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 9 LKVIQQSLEQEEAEHKATKARLAD---KNKIYESIEEAKS--EAMKEMEKKLLEERTLKQKVENLLLEAEKRcslldcdL 83
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEfrqKNGLVDLSEEAKLllQQLSELESQLAEARAELAEAEARLAALRAQ-------L 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 84 KQSQQKINELLKQKDV--LNEDVRNLTLKIEQETQKrcLTQNDLKMQT--QQVNTLkmsEKQLKQEnnhlmemkmnLEKQ 159
Cdd:COG3206 250 GSGPDALPELLQSPVIqqLRAQLAELEAELAELSAR--YTPNHPDVIAlrAQIAAL---RAQLQQE----------AQRI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 160 NAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEeceektklgkeLQQKKQELQDERDSLAAQLEITLTKADS 239
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQ-------LEARLAELPE-----------LEAELRRLEREVEVARELYESLLQRLEE 376
|
....*..
gi 109730369 240 EQLARSI 246
Cdd:COG3206 377 ARLAEAL 383
|
|
| C1_ARHGEF-like |
cd20832 |
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ... |
575-625 |
1.30e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410382 Cd Length: 53 Bit Score: 37.35 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 109730369 575 GHEFIPTLYHFPTNCEACMKPLWHMfkPPPALECRRCHIKCHKDHMDKKEE 625
Cdd:cd20832 1 GHQFVLQHYYQVTFCNHCSGLLWGI--GYQGYQCSDCEFNIHKQCIEVIEE 49
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
19-338 |
1.36e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 19 EEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERT---LKQKVENLLLEA-EKRCSLLDCDLKQSQQKINELL 94
Cdd:COG5022 852 GRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSissLKLVNLELESEIiELKKSLSSDLIENLEFKTELIA 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 95 KQKDVLNEDVRNLTLKIEQETQKrcltqndlkmqtqQVNTLKMSEKQLKQENnhlmEMKMNLEKQNAELRKERQDADGQM 174
Cdd:COG5022 932 RLKKLLNNIDLEEGPSIEYVKLP-------------ELNKLHEVESKLKETS----EEYEDLLKKSTILVREGNKANSEL 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 175 KELQDQLeaeqyfstlykTQVRELKEECEEKTKLGKELQQKKQELQderdslaaqleiTLTKADSEQlarSIAEEQYSDL 254
Cdd:COG5022 995 KNFKKEL-----------AELSKQYGALQESTKQLKELPVEVAELQ------------SASKIISSE---STELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 255 EKEKIMKELEIKEMMARHKQELTEKDATIasLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQ 334
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRRENSL--LDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLN 1126
|
....
gi 109730369 335 FEKQ 338
Cdd:COG5022 1127 LLQE 1130
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
164-434 |
1.41e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 164 RKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKL--GKELQQKKQELQDERDSLAAQLEITLTKADSEQ 241
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLrtVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 242 LARSIAEEQYSDLEKEKIMKELEIKEmmarhKQELTEKDATIASLEETNRTLTsdvanlanEKEELNNKLKDVQEQLSRl 321
Cdd:PLN02939 116 QTNSKDGEQLSDFQLEDLVGMIQNAE-----KNILLLNQARLQALEDLEKILT--------EKEALQGKINILEMRLSE- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 322 KDEEISAAAiKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEkenrklHMELKSEREKLTQQMIKYQK 401
Cdd:PLN02939 182 TDARIKLAA-QEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE------NMLLKDDIQFLKAELIEVAE 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 109730369 402 ELNEMQAQIAE----ESQIRiELQMTLDSKDSDIEQL 434
Cdd:PLN02939 255 TEERVFKLEKErsllDASLR-ELESKFIVAQEDVSKL 290
|
|
| C1_PKD2_rpt2 |
cd20843 |
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ... |
576-617 |
1.50e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410393 Cd Length: 79 Bit Score: 38.03 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHK 617
Cdd:cd20843 12 HTFVIHSYTRPTVCQFCKKLLKGLFRQ--GLQCKDCKFNCHK 51
|
|
| C1_nPKC_theta-like_rpt2 |
cd20837 |
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
576-617 |
1.60e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410387 Cd Length: 50 Bit Score: 37.03 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHK 617
Cdd:cd20837 1 HRFKVYNYMSPTFCDHCGSLLWGLFRQ--GLKCEECGMNVHH 40
|
|
| PH |
cd00821 |
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
468-550 |
1.64e-03 |
|
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 275388 [Multi-domain] Cd Length: 92 Bit Score: 38.29 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 468 LEGWLSlpVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEqSNPYMVLDIDKLFHVRPVTQtdvyradaKEIPRIFQILY 547
Cdd:cd00821 1 KEGYLL--KRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSS-YKPKGSIPLSGILEVEEVSP--------KERPHCFELVT 69
|
...
gi 109730369 548 ANE 550
Cdd:cd00821 70 PDG 72
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
121-424 |
1.66e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 121 TQNDLKMQTQQVNTLKMSE------KQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstLYKTQ 194
Cdd:PRK11281 37 TEADVQAQLDALNKQKLLEaedklvQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA------LKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 195 VRELKEECE--EKTKLGKELQQKKQELQDERDSLA---AQLeITL-TKADSEQLARSIAEEQYSDLEKEKIMKELEIKEM 268
Cdd:PRK11281 111 DEETRETLStlSLRQLESRLAQTLDQLQNAQNDLAeynSQL-VSLqTQPERAQAALYANSQRLQQIRNLLKGGKVGGKAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 269 MARHKQELTEKDATIASLEETNRTLtsdvanLANekeelNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLkTQ 348
Cdd:PRK11281 190 RPSQRVLLQAEQALLNAQNDLQRKS------LEG-----NTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRL-TL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 349 AVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREK---LTQQMIKYQKEL-NEMQAQIAEESQIRIeLQMTL 424
Cdd:PRK11281 258 SEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKlntLTQQNLRVKNWLdRLTQSERNIKEQISV-LKGSL 336
|
|
| C1_RASGRP1 |
cd20860 |
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ... |
576-631 |
1.73e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410410 Cd Length: 55 Bit Score: 37.22 E-value: 1.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHKDHmdkKEEIIAPCK 631
Cdd:cd20860 3 HNFQETTYLKPTFCDNCAGFLWGVIKQ--GYRCKDCGMNCHKQC---KDLVVFECK 53
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7-441 |
1.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 7 YQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMK---EMEKKLLEERTLKQKVENL-LLEAEKRCSLLDcd 82
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleELEERHELYEEAKAKKEELeRLKKRLTGLTPE-- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 83 lkQSQQKINELLKQKDVLNEDVRNLTLKI---EQETQKRCLTQNDLKMQTQQVNTLK---MSEKQLKQENNHLMEMKmNL 156
Cdd:PRK03918 388 --KLEKELEELEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGrelTEEHRKELLEEYTAELK-RI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 157 EKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKT--QVRELKEECEEKTKlgKELQQKKQELQDERDSLAAqleitl 234
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNL--EELEKKAEEYEKLKEKLIK------ 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 235 TKADSEQLARSIAEEQYSDLEKEKIMKEL-EIKEMMARHKQELTEKDatIASLEETNRTLtSDVANLANEKEELNNKLKD 313
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLdELEEELAELLKELEELG--FESVEELEERL-KELEPFYNEYLELKDAEKE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 314 VQEQLSRLKDEEISAAAIKAQFEKQLltertlktqavNKLAEIMNR-KEPVKRGNDTDVRRKEKENRKLHME---LKSER 389
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETE-----------KRLEELRKElEELEKKYSEEEYEELREEYLELSRElagLRAEL 682
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 109730369 390 EKLTQQMIKYQKELNEMQAQIAEESQIRIELQMtLDSKDSDIEQLRSQLQAL 441
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVKKY 733
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
33-316 |
2.00e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 33 KNKIYESIEEAKSEAMKEME-KKLLEERTlkqkvenlllEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKI 111
Cdd:pfam15905 62 KKKSQKNLKESKDQKELEKEiRALVQERG----------EQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 112 EQETQKRCLTQNDLKMQTQQvntlkmseKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLY 191
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQ--------KKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 192 KTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAA-QLEITLTKADSEQLARSIAEEQySDLEKEKIMKELEIKEMMA 270
Cdd:pfam15905 204 EEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKyKLDIAQLEELLKEKNDEIESLK-QSLEEKEQELSKQIKDLNE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 109730369 271 RHKQELTEKDATIASLEETNRTLTSDVANLaneKEELNNKLKDVQE 316
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEEL---KEKLTLEEQEHQK 325
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
130-401 |
2.16e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 130 QQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLG 209
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE-------LREEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 210 KELQQKKQELQDERDSLAAQLEITLTKADSEQLAR---SIAEEQYSDLEKE-------------------KIMKELEIKE 267
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRqqtevlspeeekelvekikELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 268 MMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEeisAAAIKAQFEKQLLTERTLKT 347
Cdd:COG1340 154 KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE---ADELHKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 109730369 348 QAVNKLAEIMNRKEPVKRgndtdvRRKEKENRKLHMELKSEREKLTQQMIKYQK 401
Cdd:COG1340 231 EIIELQKELRELRKELKK------LRKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| C1_KSR |
cd20812 |
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ... |
576-622 |
2.17e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410362 Cd Length: 48 Bit Score: 36.53 E-value: 2.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 109730369 576 HEFIPTLYhFPTNCEACMKPLWHMFKpppaleCRRCHIKCHKDHMDK 622
Cdd:cd20812 3 HRFSKKLF-MRQTCDYCHKQMFFGLK------CKDCKYKCHKKCAKK 42
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-437 |
2.31e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 156 LEKQNAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLE---- 231
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 232 -ITLTKADSEQLARSIAEEQYSDLEKEKIMKELEikEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNK 310
Cdd:PRK02224 336 aAQAHNEEAESLREDADDLEERAEELREEAAELE--SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 311 LKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLktQAVNKLAEIMNRKEPVKRGNDTDVRRKEKEnrklhmELKSERE 390
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEAL--LEAGKCPECGQPVEGSPHVETIEEDRERVE------ELEAELE 485
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 109730369 391 KLTQQMIKYQKELNEMQAQIAEESQIRielqmTLDSKDSDIEQLRSQ 437
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIE-----RLEERREDLEELIAE 527
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8-419 |
2.36e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 8 QLKVIQQSLEQEEAEHKATKARLADK-----NKIYESIEEAK-SEAMKEMEKKLLEERTLKQKVENLLL-----EAEKRC 76
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKhtqalEELTEQLEQAKrNKANLEKAKQALESENAELQAELRTLqqakqDSEHKR 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 77 SLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIE------QETQKRCL---------------TQNDLKMQTQQVNTL 135
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsvssllNEAEGKNIklskdvsslesqlqdTQELLQEETRQKLNL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 136 KMSEKQLKQENNHLMEM-------KMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKL 208
Cdd:pfam01576 488 STRLRQLEDERNSLQEQleeeeeaKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 209 GKELQQKKQELQDERDSLAAQLE-----ITLTKADSEQLARSIAEE-----QYSDlEKEKIMKELEIKEM----MARHKQ 274
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDhqrqlVSNLEKKQKKFDQMLAEEkaisaRYAE-ERDRAEAEAREKETralsLARALE 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 275 ELTEkdaTIASLEETNRTLTSDVANLANEKEE--------------LNNKLKDVQEQLSRLKDE-----------EISAA 329
Cdd:pfam01576 647 EALE---AKEELERTNKQLRAEMEDLVSSKDDvgknvhelerskraLEQQVEEMKTQLEELEDElqatedaklrlEVNMQ 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 330 AIKAQFEKqlltertlktqavnklaEIMNRKEPvkrgNDTDVRRKEKENRKLHMELKSEREKLTQQMI---KYQKELNEM 406
Cdd:pfam01576 724 ALKAQFER-----------------DLQARDEQ----GEEKRRQLVKQVRELEAELEDERKQRAQAVAakkKLELDLKEL 782
|
490
....*....|...
gi 109730369 407 QAQIAEESQIRIE 419
Cdd:pfam01576 783 EAQIDAANKGREE 795
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
46-413 |
2.41e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 46 EAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQEtqkrcltQNDL 125
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL-------KNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 126 KMQTQQVNTLKMSEKQLK--QENNHLMEmKMNLEKQNAELRKERQDADGQMKELQdqleaeqyfstLYKTQVRELKEECE 203
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAKvcLTDVTIME-RFQMELKDVERKIAQQAAKLQGSDLD-----------RTVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 204 EKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMarhkQELTEKDATI 283
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI----REIKDAKEQD 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 284 ASLEETNRTLTSDVANLANEKEELNNKLKD-VQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEP 362
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDkVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEK 991
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 109730369 363 VKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQ-KELNEMQAQIAEE 413
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENElKEVEEELKQHLKE 1043
|
|
| C1_Raf |
cd20811 |
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ... |
576-617 |
3.23e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410361 Cd Length: 49 Bit Score: 36.12 E-value: 3.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKpppaleCRRCHIKCHK 617
Cdd:cd20811 3 HNFVRKTFFTLAFCDVCRKLLFQGFR------CQTCGFKFHQ 38
|
|
| C1_Myosin-IXb |
cd20884 |
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ... |
573-634 |
3.31e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410434 Cd Length: 58 Bit Score: 36.38 E-value: 3.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109730369 573 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHKDHMDKkeeIIAPCKVYY 634
Cdd:cd20884 3 YNGHVFTSYQVNIMQSCEQCSSYIWAMEK---ALLCSVCKMTCHKKCLSK---IQSHCSSTC 58
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
274-443 |
3.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 274 QELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDeeisAAAIKAQFEKQLLTERTLKtQAVNKL 353
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELA-ELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 354 AEIMNRKEPVKRgNDTDVRRKEKENRKLHMELKSEREKLT----QQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDS 429
Cdd:COG4717 149 EELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....
gi 109730369 430 DIEQLRSQLQALHI 443
Cdd:COG4717 228 ELEQLENELEAAAL 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-279 |
3.56e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 1 MEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIY---ESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCS 77
Cdd:pfam02463 746 DEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKtekLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIE 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 78 LLDC----DLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEmk 153
Cdd:pfam02463 826 QEEKikeeELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE-- 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 154 mNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTklgKELQQKKQELQDERDSLAAQLEIT 233
Cdd:pfam02463 904 -EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK---EEEEERNKRLLLAKEELGKVNLMA 979
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 109730369 234 LTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEK 279
Cdd:pfam02463 980 IEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
19-283 |
4.01e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 19 EEAEhKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLK----------------QKVENLLLEAEKRCSLLDCD 82
Cdd:pfam17380 319 EEAE-KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRElerirqeeiameisrmRELERLQMERQQKNERVRQE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 83 LKQS-QQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNA 161
Cdd:pfam17380 398 LEAArKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 162 ELRKERQD----ADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERdslaAQLEITLTKA 237
Cdd:pfam17380 478 ELEKEKRDrkraEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR----KQQEMEERRR 553
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 109730369 238 DSEQLARSIAEEQYSD-LEKEKIMKELEIKEMMARHKQELTEKDATI 283
Cdd:pfam17380 554 IQEQMRKATEERSRLEaMEREREMMRQIVESEKARAEYEATTPITTI 600
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
30-419 |
4.40e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 30 LADKNKIYESIEEAKSEAM---KEMEKKLLEE-RTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVlNEDVR 105
Cdd:TIGR01612 1199 IAEIEKDKTSLEEVKGINLsygKNLGKLFLEKiDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDI-KAEME 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 106 NLTLKIEQETQKRCLTQ-NDLKMQTQQVNTLKMSEKQLKQENnhLMEMKMNLEKQNAELRKERQDADGQMKELQDqleae 184
Cdd:TIGR01612 1278 TFNISHDDDKDHHIISKkHDENISDIREKSLKIIEDFSEESD--INDIKKELQKNLLDAQKHNSDINLYLNEIAN----- 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 185 qYFSTLYKTQVRELKEECEEKTklgKELQQKKQELQDERDslaaqleitltkaDSEQLARSIAEEQYSDLEKEKIMKELE 264
Cdd:TIGR01612 1351 -IYNILKLNKIKKIIDEVKEYT---KEIEENNKNIKDELD-------------KSEKLIKKIKDDINLEECKSKIESTLD 1413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 265 ----------IKEMMARHKQELTEKDATIASLEETNRTLTSDVAN--LANEKEEL------NNKLKDVQEQLSRLKDEEI 326
Cdd:TIGR01612 1414 dkdidecikkIKELKNHILSEESNIDTYFKNADENNENVLLLFKNieMADNKSQHilkikkDNATNDHDFNINELKEHID 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 327 SAAAIKAQFE---KQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKEnrKLHMELKSEREKLTQQMIKYQKEL 403
Cdd:TIGR01612 1494 KSKGCKDEADknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSE--IIIKEIKDAHKKFILEAEKSEQKI 1571
|
410
....*....|....*.
gi 109730369 404 NEMQAQiaeesQIRIE 419
Cdd:TIGR01612 1572 KEIKKE-----KFRIE 1582
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
20-326 |
4.57e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 20 EAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENL---LLEAEKRCSLLDCDLKQSQQKINELLKQ 96
Cdd:PLN02939 85 ELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLvgmIQNAEKNILLLNQARLQALEDLEKILTE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 97 KDVLNEDVRNLTLKIEQetqkrclTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKE 176
Cdd:PLN02939 165 KEALQGKINILEMRLSE-------TDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENML 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 177 LQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQD-ERDSLAAQLEItlTKADSEQLARSIAEEQYSDLE 255
Cdd:PLN02939 238 LKDDIQF-------LKAELIEVAETEERVFKLEKERSLLDASLRElESKFIVAQEDV--SKLSPLQYDCWWEKVENLQDL 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109730369 256 KEKIMKELEIKEMMARHKQELTEK-DATIASLEETNrtltsdVANLANEKEEL-NNKLKDVQEQLSRlKDEEI 326
Cdd:PLN02939 309 LDRATNQVEKAALVLDQNQDLRDKvDKLEASLKEAN------VSKFSSYKVELlQQKLKLLEERLQA-SDHEI 374
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
57-182 |
4.64e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.43 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 57 EERTLKQKVENLLLEAEKrcslLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLK 136
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKEN----LEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLE 757
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 109730369 137 MSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLE 182
Cdd:pfam05911 758 TRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE 803
|
|
| C1_PKD1_rpt2 |
cd20842 |
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ... |
576-617 |
5.08e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410392 Cd Length: 94 Bit Score: 36.92 E-value: 5.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHK 617
Cdd:cd20842 35 HTFVIHSYTRPTVCQYCKKLLKGLFR--QGLQCKDCKFNCHK 74
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
91-358 |
5.28e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 91 NELLKQK-DVLNEDVRNLTLKIEQETQKrCLTQNDLKMQTQQVNTLKMSEKQLKQENnHLMEMKmNLEKQNAELRKERQD 169
Cdd:PHA02562 169 DKLNKDKiRELNQQIQTLDMKIDHIQQQ-IKTYNKNIEEQRKKNGENIARKQNKYDE-LVEEAK-TIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 170 ADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLG---------KELQQKKQELQDERDSLAAQLEITLTKADSE 240
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 241 QLARSIAEEQysdlekekIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSR 320
Cdd:PHA02562 326 EEIMDEFNEQ--------SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
250 260 270
....*....|....*....|....*....|....*...
gi 109730369 321 LKDEEisaaaIKAQFEKQLLTERTLKTQAVNKLAEIMN 358
Cdd:PHA02562 398 LVKEK-----YHRGIVTDLLKDSGIKASIIKKYIPYFN 430
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
52-257 |
5.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 52 EKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLK----- 126
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 127 MQTQ---------------------QVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEaeq 185
Cdd:COG3883 95 LYRSggsvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA--- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109730369 186 yfstlyktqvrELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKE 257
Cdd:COG3883 172 -----------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| C1_TNS2-like |
cd20826 |
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ... |
574-630 |
5.40e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410376 Cd Length: 52 Bit Score: 35.44 E-value: 5.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 109730369 574 KGHEFIPTLYHFPTNCEACMKPLWHmfkppPALECRRCHIKCHKDHmdkKEEIIAPC 630
Cdd:cd20826 1 KSHSFKEKSFRKPRTCDVCKQIIWN-----EGSSCRVCKYACHRKC---EPKVTAAC 49
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
211-355 |
5.71e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 211 ELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKqELTEKDATIASLEETN 290
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109730369 291 rTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAE 355
Cdd:COG1579 93 -ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-442 |
6.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 192 KTQVRELKEECEEKTKlgKELQQKKQELQDERDSLAAQLEITLTKadseqlaRSIAEEQYSDLEkekimkeleikEMMAR 271
Cdd:PRK02224 186 RGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQ-------REQARETRDEAD-----------EVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 272 HKQELTEkdatIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE-----------EISAAAIKAQFE---- 336
Cdd:PRK02224 246 HEERREE----LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagldDADAEAVEARREeled 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 337 -----KQLLTERTLKTQAVNKLAEIMnrkepvkRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIA 411
Cdd:PRK02224 322 rdeelRDRLEECRVAAQAHNEEAESL-------REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270
....*....|....*....|....*....|.
gi 109730369 412 EESQIRIELQMTLDSKDSDIEQLRSQLQALH 442
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
52-333 |
6.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 52 EKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQ 131
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 132 VNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKE 211
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 212 LQQKKQELQDE--RDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEET 289
Cdd:COG4372 169 LEQELQALSEAeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 109730369 290 NRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKA 333
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
266-402 |
6.90e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 266 KEMMARHKQELtekDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEisaAAIKAQFEKQLltertl 345
Cdd:PRK00409 508 KKLIGEDKEKL---NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEA------ 575
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109730369 346 kTQAVNKL----AEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSErEKLTQQMIKYQKE 402
Cdd:PRK00409 576 -QQAIKEAkkeaDEIIKELRQLQKGGYASVKAHELIEARKRLNKANE-KKEKKKKKQKEKQ 634
|
|
| C1_RASGRP4 |
cd20863 |
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 ... |
576-621 |
7.03e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 (RASGRP4) and similar proteins; RASGRP4 functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. It may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410413 Cd Length: 57 Bit Score: 35.52 E-value: 7.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 109730369 576 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMD 621
Cdd:cd20863 4 HNFHETTFKKPTFCDSCSGFLWGVTK--QGYRCQDCGINCHKHCKD 47
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
191-279 |
8.32e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 191 YKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEqlARSIAEEQYSDLEKEKIMKELEIKEmma 270
Cdd:PRK00409 532 LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKE--AKKEADEIIKELRQLQKGGYASVKA--- 606
|
....*....
gi 109730369 271 rhkQELTEK 279
Cdd:PRK00409 607 ---HELIEA 612
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
151-405 |
8.61e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 39.24 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 151 EMKMNLEKQNAELRKERQDAD---GQMKELQDQLEAEQyfSTLYKTQVRELKeecEEKTKLGKELQQKKQEL---QDERD 224
Cdd:pfam05701 81 ELKLNLERAQTEEAQAKQDSElakLRVEEMEQGIADEA--SVAAKAQLEVAK---ARHAAAVAELKSVKEELeslRKEYA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 225 SLAAQLEITLTKADSeqlarSIAEEQysdlEKEKIMKELEIkEMMARhKQELTEKDATIASLEETNRTltsdvANLANEK 304
Cdd:pfam05701 156 SLVSERDIAIKRAEE-----AVSASK----EIEKTVEELTI-ELIAT-KESLESAHAAHLEAEEHRIG-----AALAREQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 305 EELN--NKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKtqavnklAEIMNRKEPVKRGNDTDVRRKEKENRKLH 382
Cdd:pfam05701 220 DKLNweKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLK-------AELAAYMESKLKEEADGEGNEKKTSTSIQ 292
|
250 260
....*....|....*....|...
gi 109730369 383 MELKSEREKLTQQMIKYQKELNE 405
Cdd:pfam05701 293 AALASAKKELEEVKANIEKAKDE 315
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
93-309 |
9.19e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 38.75 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 93 LLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMS----EKQLKQENNHLMEMKMNLEKQNAELRKE-- 166
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLArvdlEAKIESLKEELAFLKKNHEEEVRELQAQvs 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 167 ------------RQDADGQMKELQDQLE--AEQYFSTL---YKTQVRELKEECEektKLGKELQQKKQELQDER---DSL 226
Cdd:pfam00038 153 dtqvnvemdaarKLDLTSALAEIRAQYEeiAAKNREEAeewYQSKLEELQQAAA---RNGDALRSAKEEITELRrtiQSL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 227 AAQLEitltkadseqlarsiaeeqysDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEE 306
Cdd:pfam00038 230 EIELQ---------------------SLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQE 288
|
...
gi 109730369 307 LNN 309
Cdd:pfam00038 289 LLN 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
264-412 |
9.45e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109730369 264 EIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIK--AQFEKQLLT 341
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109730369 342 ERTLKTQAVNKLAEIMNRKEPVKrgndTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAE 412
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELE----EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| |
